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ZNUC_HAES1
ID   ZNUC_HAES1              Reviewed;         264 AA.
AC   Q0I4A9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=HS_1037;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25312.1; -; Genomic_DNA.
DR   RefSeq; WP_011609192.1; NC_008309.1.
DR   AlphaFoldDB; Q0I4A9; -.
DR   SMR; Q0I4A9; -.
DR   STRING; 205914.HS_1037; -.
DR   EnsemblBacteria; ABI25312; ABI25312; HS_1037.
DR   KEGG; hso:HS_1037; -.
DR   eggNOG; COG1121; Bacteria.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; GHDHVHP; -.
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; Translocase; Transport; Zinc; Zinc transport.
FT   CHAIN           1..264
FT                   /note="Zinc import ATP-binding protein ZnuC"
FT                   /id="PRO_0000281510"
FT   DOMAIN          11..226
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ   SEQUENCE   264 AA;  29367 MW;  C8A7E7EAF1B4DB97 CRC64;
     MQIHSLKYPL IELKGVNVTF AQKTILSDIN LTIYPNSIMT IVGPNGGGKS TLLKVLLKLL
     PATSGKVIYS KNVVIGYVPQ NIYLDKSLPI TVEKFLSLRK GTHKQDIKDA LTLLSIGHLR
     LNAMQKLSGG EMQRVLLARA ILNKPNLLVL DEPTQGVDIT GQAELYQLIK QTQQQLNCAI
     LMVSHDLHLV MADTNEVLCV NQHICCAGSP EAVSNDPVFI RFFGNQFAKN IAFYTHHHNH
     KHNIHGDICC GQDFRSTQCK HKIN
 
 
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