ID   MODA_MYCTO              Reviewed;         261 AA.
AC   P9WGU2; 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 41.
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=MT1905;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46176.1; -; Genomic_DNA.
DR   PIR; A70666; A70666.
DR   RefSeq; WP_003409326.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGU2; -.
DR   SMR; P9WGU2; -.
DR   EnsemblBacteria; AAK46176; AAK46176; MT1905.
DR   KEGG; mtc:MT1905; -.
DR   PATRIC; fig|83331.31.peg.2049; -.
DR   HOGENOM; CLU_065520_0_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
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: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   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Metal-binding; Molybdenum; Palmitate;
KW   Signal; Transport; Tungsten.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000305"
FT   CHAIN           22..261
FT                   /note="Molybdate-binding protein ModA"
FT                   /id="PRO_0000428302"
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"
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