ompW protein (Azoarcus sp. BH72) - STRING interaction network

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ompW

Outer membrane protein W precursor. Acts as a receptor for colicin S4; High confidence in function and specificity. (246 aa)

Predicted Functional Partners:

hemN

0.893

ccoO

0.842

azo2831

0.779

ccoN

0.768

ccoP

0.580

azo3096

0.574

azo3085

0.569

ccoG

0.562

rdxA

0.555

rdxB

0.555

Your Current Organism:

Azoarcus sp. BH72

NCBI taxonomy Id: 62928
Other names: A. sp. BH72

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
azo2831	azo3085	azo2831	azo3085	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	0.434
azo2831	azo3096	azo2831	azo3096	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	0.529
azo2831	ccoG	azo2831	azo1345	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...]	0.529
azo2831	ccoN	azo2831	azo1341	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot\|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...]	0.513
azo2831	ccoO	azo2831	azo1342	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl\|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...]	0.574
azo2831	ccoP	azo2831	azo1344	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.	0.430
azo2831	hemN	azo2831	azo1352	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Oxygen-independent coproporphyrinogen III oxidase. ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO PROTOPORPHYRINOGEN-IX. hemN: oxygen-independent coproporphyrinogen III oxidase; High confidence in function and specificity.	0.656
azo2831	ompW	azo2831	azo3741	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Outer membrane protein W precursor. Acts as a receptor for colicin S4; High confidence in function and specificity.	0.779
azo2831	rdxA	azo2831	azo2476	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to rdxA of R. sphaeroides of 37% (SWISSPROT:RDXA_RHOSH) Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain Probable 5 TMHs no signal peptide; Family membership.	0.529
azo2831	rdxB	azo2831	azo3100	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to rdxB of R. sphaeroides of 39% (sprot\|RDXB_RHOSH). Involved in a membrane generated redox signal; required to maintain repression of photosynthesis gene expression in the presence of oxygen. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4Fe-4S binding doamin no signal peptide probable 5 TMHs; Family membership.	0.529
azo3085	azo2831	azo3085	azo2831	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	0.434
azo3085	azo3096	azo3085	azo3096	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	0.709
azo3085	ccoO	azo3085	azo1342	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl\|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...]	0.989
azo3085	ccoP	azo3085	azo1344	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.	0.771
azo3085	ompW	azo3085	azo3741	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	Outer membrane protein W precursor. Acts as a receptor for colicin S4; High confidence in function and specificity.	0.569
azo3096	azo2831	azo3096	azo2831	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.	0.529
azo3096	azo3085	azo3096	azo3085	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	Conserved hypothetical membrane protein. Homology to CV2709 of Chromobacterium violaceum of 40% (trembl\|Q7NUI9). Has PF04550;Phage holin family 2:Holins are a diverse family of proteins that cause bacterial membrane lysis during late-protein synthesis. It is thought that the temporal precision of holin-mediated lysis may occur through the buildup of a holin oligomer which causes the lysis. IPR007633;Phage_holin_2. TMHMM2 reporting 12 TMH's Present. no signal peptide; Conserved hypothetical protein.	0.709
azo3096	ccoN	azo3096	azo1341	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	Probable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot\|COX1_RHOCA). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...]	0.761
azo3096	ccoO	azo3096	azo1342	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl\|Q8KS21). CYTOCHROME C OXIDASE IS THE COMPONENT OF THE RESPIRATORY CHAIN THAT CATALYZES THE REDUCTION OF OXYGEN TO WATER. SUBUNITS 1- 3 FORM THE FUNCTIONAL CORE OF THE ENZYME COMPLEX. CO I IS THE CATALYTIC SUBUNIT OF THE ENZYME. ELECTRONS ORIGINATING IN CYTOCHROME C OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...]	0.772
azo3096	ccoP	azo3096	azo1344	Conserved hypothetical iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to pbprb0648 of P. profundum (tremblnew\|CAG22521). Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain no signal peptide 4 TMHs; Conserved hypothetical protein.	Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.	0.766