MODC_MYCTU
ID MODC_MYCTU Reviewed; 369 AA.
AC P9WQL3; L0TAL9; O05126; P95155;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Molybdenum import ATP-binding protein ModC {ECO:0000255|HAMAP-Rule:MF_01705};
DE EC=7.3.2.5 {ECO:0000255|HAMAP-Rule:MF_01705};
GN Name=modC {ECO:0000255|HAMAP-Rule:MF_01705}; OrderedLocusNames=Rv1859;
GN ORFNames=MTCY359.14;
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 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: Part of the ABC transporter complex ModABC involved in
CC molybdenum import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) +
CC phosphate; Xref=Rhea:RHEA:22020, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36264,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01705};
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:0000255|HAMAP-Rule:MF_01705}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01705};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01705}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate
CC importer (TC 3.A.1.8) family. {ECO:0000255|HAMAP-Rule:MF_01705}.
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DR EMBL; X99258; CAA67644.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44625.1; -; Genomic_DNA.
DR PIR; C70666; C70666.
DR RefSeq; NP_216375.1; NC_000962.3.
DR RefSeq; WP_003899051.1; NZ_NVQJ01000013.1.
DR AlphaFoldDB; P9WQL3; -.
DR SMR; P9WQL3; -.
DR STRING; 83332.Rv1859; -.
DR TCDB; 3.A.1.8.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; P9WQL3; -.
DR DNASU; 885731; -.
DR GeneID; 885731; -.
DR KEGG; mtu:Rv1859; -.
DR TubercuList; Rv1859; -.
DR eggNOG; COG1118; Bacteria.
DR OMA; HDPLDAM; -.
DR PhylomeDB; P9WQL3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015412; F:ABC-type molybdate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR004606; Mop_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005116; Transp-assoc_OB_typ1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03459; TOBE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51241; MODC; 1.
DR PROSITE; PS51866; MOP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Molybdenum; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..369
FT /note="Molybdenum import ATP-binding protein ModC"
FT /id="PRO_0000092565"
FT DOMAIN 4..239
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT DOMAIN 293..361
FT /note="Mop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT CONFLICT 51..111
FT /note="DAGLVRLGDRVLTDTEAGVNVATHDRRVGLLLQDPLLFPHLSVAKNVAFGPQ
FT CRRGMFGSG -> RRGLGTFGGPGVDRHRGRGECGDPRPSSRAAVARPVVVSTPERGQK
FT RGLRTTMPSRDVWVRA (in Ref. 1; CAA67644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 38610 MW; D931CC447E70FBD4 CRC64;
MSKLQLRAVV ADRRLDVEFS VSAGEVLAVL GPNGAGKSTA LHVIAGLLRP DAGLVRLGDR
VLTDTEAGVN VATHDRRVGL LLQDPLLFPH LSVAKNVAFG PQCRRGMFGS GRARTRASAL
RWLREVNAEQ FADRKPRQLS GGQAQRVAIA RALAAEPDVL LLDEPLTGLD VAAAAGIRSV
LRSVVARSGC AVVLTTHDLL DVFTLADRVL VLESGTIAEI GPVADVLTAP RSRFGARIAG
VNLVNGTIGP DGSLRTQSGA HWYGTPVQDL PTGHEAIAVF PPTAVAVYPE PPHGSPRNIV
GLTVAEVDTR GPTVLVRGHD QPGGAPGLAA CITVDAATEL RVAPGSRVWF SVKAQEVALH
PAPHQHASS
