MODA_MYCTU
ID MODA_MYCTU Reviewed; 261 AA.
AC P9WGU3; L0T833; O05125; P0A5Y0; P95157;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Molybdate-binding protein ModA {ECO:0000305};
DE AltName: Full=Molybdate/tungstate-binding protein ModA {ECO:0000305};
DE Flags: Precursor;
GN Name=modA; OrderedLocusNames=Rv1857; ORFNames=MTCY359.16c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RA Laqueyrerie A.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Involved in the transport of molybdenum into the cell. Part
CC of the binding-protein-dependent transport system ModABCD (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ModC),
CC two transmembrane proteins (ModB) and a solute-binding protein (ModA).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC family. {ECO:0000305}.
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DR EMBL; X99258; CAA67642.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44623.1; -; Genomic_DNA.
DR PIR; A70666; A70666.
DR RefSeq; NP_216373.1; NC_000962.3.
DR RefSeq; WP_003409326.1; NZ_NVQJ01000013.1.
DR AlphaFoldDB; P9WGU3; -.
DR SMR; P9WGU3; -.
DR STRING; 83332.Rv1857; -.
DR TCDB; 3.A.1.8.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; P9WGU3; -.
DR DNASU; 885655; -.
DR GeneID; 885655; -.
DR KEGG; mtu:Rv1857; -.
DR TubercuList; Rv1857; -.
DR eggNOG; COG0725; Bacteria.
DR OMA; VCAPQVP; -.
DR PhylomeDB; P9WGU3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030973; F:molybdate ion binding; ISS:UniProtKB.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR InterPro; IPR005950; ModA.
DR PIRSF; PIRSF004846; ModA; 1.
DR TIGRFAMs; TIGR01256; modA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Metal-binding; Molybdenum; Palmitate;
KW Reference proteome; Signal; Transport; Tungsten.
FT SIGNAL 1..21
FT /evidence="ECO:0000305"
FT CHAIN 22..261
FT /note="Molybdate-binding protein ModA"
FT /id="PRO_0000031831"
FT BINDING 48
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 76
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 179
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT BINDING 197
FT /ligand="molybdate"
FT /ligand_id="ChEBI:CHEBI:36264"
FT /evidence="ECO:0000250|UniProtKB:P37329"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 1..59
FT /note="MRWIGLSTGLVSAMLVAGLVACGSNSPASSPAGPTQGARSIVVFAAASLQSA
FT FTQIGEQ -> MWIEFTRIVASRADAGCPVDRGVRGCLAAVCVSLRSVSM (in Ref.
FT 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..134
FT /note="MDSVAKAGLLAGHPTNFATNTMVIVAAAGNPKKIR -> IGQCGQGGVAGRS
FT SDKLRHQHDGHRCRRRQSQEDP (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 26576 MW; CFE292F6D595A9F5 CRC64;
MRWIGLSTGL VSAMLVAGLV ACGSNSPASS PAGPTQGARS IVVFAAASLQ SAFTQIGEQF
KAGNPGVNVN FAFAGSSELA TQLTQGATAD VFASADTAQM DSVAKAGLLA GHPTNFATNT
MVIVAAAGNP KKIRSFADLT RPGLNVVVCQ PSVPCGSATR RIEDATGIHL NPVSEELSVT
DVLNKVITGQ ADAGLVYVSD ALSVATKVTC VRFPEAAGVV NVYAIAVLKR TSQPALARQF
VAMVTAAAGR RILDQSGFAK P
