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Rv1273c Rv1273c Rv0194 Rv0194 Rv1272c Rv1272c irtA irtA irtB irtB cydC cydC cydD cydD
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Rv1273cRv1273c, (MTCY50.09), len: 582 aa. Probable drugs-transport transmembrane ATP-binding protein ABC transporter (see citation below), similar to e.g. YWJA_BACSU|P45861 hypothetical abc transporter from B. subtilis (575 aa), FASTA scores: opt: 810, E(): 0, (27.0% identity in 578 aa overlap); etc. Contains PS00136 Serine proteases, subtilase family, aspartic acid active site; 2 x PS00211 ABC transporters family signature; and PS00017 ATP/GTP-binding site motif A (P-loop). Belongs to the ATP-binding transport protein family (ABC transporters),MSBA subfamily. (582 aa)
Rv0194Probable transmembrane multidrug efflux pump; Overexpression in M. smegmatis increases resistance to erythromycin, ampicillin, novobiocin and vancomycin. It also reduces accumulation of ethidium bromide in the cell. Belongs to the ABC transporter superfamily. Lipid exporter (TC 3.A.1.106) family. (1194 aa)
Rv1272cProbable drugs-transport transmembrane ATP-binding protein ABC transporter; ABC transporter involved in fatty acid import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). (631 aa)
irtAIron-regulated transporter IrtA; Part of the ABC transporter complex IrtAB involved in iron import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for replication in human macrophages and in mouse lungs. (859 aa)
irtBIron-regulated transporter IrtB; Part of the ABC transporter complex IrtAB involved in iron import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for replication in human macrophages and in mouse lungs. Belongs to the ABC transporter superfamily. Siderophore- Fe(3+) uptake transporter (SIUT) (TC 3.A.1.21) family. (579 aa)
cydCRv1620c, (MTCY01B2.12c), len: 576 aa. Probable cydC,transmembrane ATP-binding protein ABC transporter involved in transport of component linked with the assembly of cytochrome (see citation below), similar to others e.g. CYDC_ECOLI|P23886 transport ATP-binding protein from Escherichia coli (573 aa), FASTA scores: opt: 631, E(): 1.6e-30, (28.5% identity in 569 aa overlap); C-terminal part of AL034355|SCD78_14 from Streptomyces coelicolor (1172 aa), FASTA scores: opt: 956, E(): 0, (38.8% identity in 554 aa overlap); etc. Contains (PS00211) ABC transporters family signature, and (PS00017) [...] (576 aa)
cydDRv1621c, (MTCY01B2.13c), len: 527 aa. Probable cydD,transmembrane ATP-binding protein ABC transporter involved in transport of component linked with the assembly of cytochrome (see citation below), similar to others e.g. P94366|CYDC_BACSU transport ATP-binding protein from Bacillus subtilis (567 aa), FASTA scores: opt: 784, E(): 0,(30.1% identity in 535 aa overlap); N-terminal part of AL034355|SCD78_14 from Streptomyces coelicolor (1172 aa),FASTA scores: opt: 1295, E(): 0, (44.6% identity in 534 aa overlap); etc. Also similar to Q11019|Y07D_MYCTU from Mycobacterium tuberculosis (579 aa [...] (527 aa)
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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