MODA_MYCBO
ID MODA_MYCBO Reviewed; 261 AA.
AC P0A5Y1; A0A1R3XZI8; O05125; P95157; X2BIP4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BQ2027_MB1888;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Involved in the transport of molybdenum into the cell. Part
CC of the binding-protein-dependent transport system ModABCD.
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; LT708304; SIU00492.1; -; Genomic_DNA.
DR RefSeq; NP_855540.1; NC_002945.3.
DR RefSeq; WP_003409326.1; NC_002945.4.
DR AlphaFoldDB; P0A5Y1; -.
DR SMR; P0A5Y1; -.
DR EnsemblBacteria; SIU00492; SIU00492; BQ2027_MB1888.
DR PATRIC; fig|233413.5.peg.2069; -.
DR OMA; VCAPQVP; -.
DR Proteomes; UP000001419; 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_0000031830"
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