MODC2_AZOVI
ID MODC2_AZOVI Reviewed; 358 AA.
AC Q44538;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Molybdenum import ATP-binding protein ModC 2 {ECO:0000255|HAMAP-Rule:MF_01705};
DE EC=7.3.2.5 {ECO:0000255|HAMAP-Rule:MF_01705};
GN Name=modC2 {ECO:0000255|HAMAP-Rule:MF_01705};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT "Physical and genetic map of the major nif gene cluster from Azotobacter
RT vinelandii.";
RL J. Bacteriol. 171:1017-1027(1989).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01705}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; M20568; AAA64722.1; -; Genomic_DNA.
DR RefSeq; WP_012698850.1; NZ_FPKM01000020.1.
DR AlphaFoldDB; Q44538; -.
DR SMR; Q44538; -.
DR OMA; RINHIEI; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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:0042888; F:molybdenum ion transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR015852; ABC_transpr_ModC.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR011868; ModC_ABC_ATP-bd.
DR InterPro; IPR004606; Mop_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005116; Transp-assoc_OB_typ1.
DR PANTHER; PTHR43514:SF9; PTHR43514:SF9; 1.
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 TIGRFAMs; TIGR02142; modC_ABC; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51241; MODC; 1.
DR PROSITE; PS51866; MOP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane; Molybdenum;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..358
FT /note="Molybdenum import ATP-binding protein ModC 2"
FT /id="PRO_0000092529"
FT DOMAIN 1..234
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
FT DOMAIN 293..358
FT /note="Mop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01705"
SQ SEQUENCE 358 AA; 39648 MW; 8117314F6B29BADD CRC64;
MPEQGIEAQL RLQRGAFRLD AHLQLPANGI SVLLGRSGSG KTTLLRAIAG LERAEGFLQV
GGQLWQDATC FRPPHQRSLG YVRQASELLP HLDVRANLEF GYRRIPRARR RLGLDEVIAL
FGLEDLLDQR AEWLPNGPRQ RVAIACALLT SPDLLLLDAP LICLDRHSRA QILPALEQLR
GQLRIPLLYV THSQDEVTRL ADHLILLDKG KTFASGPPGR LLSDPRLPLN HPDEAAVVLI
GQVEHHDPHY RLSTVRVPGG TLSVSLSRLP PGAETRVRIF ARDVSLSLDP PHNSSILNIL
RVRIADLFHE QDSARVMVRL DLDSACILAR ITRLSADRLG LAPGLQVYAQ IKSVALME