ZNUC_AERHH
ID ZNUC_AERHH Reviewed; 254 AA.
AC A0KPH6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Zinc import ATP-binding protein ZnuC {ECO:0000255|HAMAP-Rule:MF_01725};
DE EC=7.2.2.20 {ECO:0000255|HAMAP-Rule:MF_01725};
GN Name=znuC {ECO:0000255|HAMAP-Rule:MF_01725}; OrderedLocusNames=AHA_3729;
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
CC -!- FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc
CC import. Responsible for energy coupling to the transport system.
CC {ECO:0000255|HAMAP-Rule:MF_01725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) +
CC phosphate(in) + Zn(2+)(in); Xref=Rhea:RHEA:29795, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29105, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01725};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ZnuC),
CC two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).
CC {ECO:0000255|HAMAP-Rule:MF_01725}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01725}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01725}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Zinc importer
CC (TC 3.A.1.15.5) family. {ECO:0000255|HAMAP-Rule:MF_01725}.
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DR EMBL; CP000462; ABK37975.1; -; Genomic_DNA.
DR RefSeq; WP_011707444.1; NC_008570.1.
DR RefSeq; YP_858177.1; NC_008570.1.
DR AlphaFoldDB; A0KPH6; -.
DR SMR; A0KPH6; -.
DR STRING; 380703.AHA_3729; -.
DR EnsemblBacteria; ABK37975; ABK37975; AHA_3729.
DR KEGG; aha:AHA_3729; -.
DR PATRIC; fig|380703.7.peg.3703; -.
DR eggNOG; COG1121; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; GHDHVHP; -.
DR Proteomes; UP000000756; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015633; F:ABC-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR017882; ZnuC.
DR PANTHER; PTHR42734:SF9; PTHR42734:SF9; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51298; ZNUC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..254
FT /note="Zinc import ATP-binding protein ZnuC"
FT /id="PRO_0000281489"
FT DOMAIN 5..219
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT REGION 233..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ SEQUENCE 254 AA; 28323 MW; 6F73C57F9F9B214E CRC64;
MTQLVELKEV CLSFDGRSVL DKVSFTLNKG KITTLVGPNG AGKSTLSKLV LGLLTPDSGQ
ITRSRDLRVG YVPQRLYLDP TLPLTVRRFL QLGKNGRLSI EEALNRVGAE DLLDNRMQKL
SGGEMQRVLL ARALLVKPEL LVLDEPVQGV DINGQIELYA LISQLAAEFN CAVLMVSHDL
HLVMASTHEV ICLNRHVCCH GEPESVARHP EFARLFGRPE QEVLAVYTHH HHCDGEHHHH
EPQVPVIRLP SRNQ