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Y290_HAEIN
ID   Y290_HAEIN              Reviewed;         722 AA.
AC   P77868;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Probable cation-transporting ATPase HI_0290;
DE            EC=7.2.2.-;
GN   OrderedLocusNames=HI_0290;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; L42023; AAC21955.1; -; Genomic_DNA.
DR   RefSeq; NP_438457.1; NC_000907.1.
DR   RefSeq; WP_010868972.1; NC_000907.1.
DR   STRING; 71421.HI_0290; -.
DR   EnsemblBacteria; AAC21955; AAC21955; HI_0290.
DR   KEGG; hin:HI_0290; -.
DR   PATRIC; fig|71421.8.peg.306; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_11_2_6; -.
DR   OMA; ITFFGWM; -.
DR   PhylomeDB; P77868; -.
DR   BioCyc; HINF71421:G1GJ1-308-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR   GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00403; HMA; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..722
FT                   /note="Probable cation-transporting ATPase HI_0290"
FT                   /id="PRO_0000046334"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        675..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        697..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          9..75
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        422
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         23
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         617
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         621
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
SQ   SEQUENCE   722 AA;  78072 MW;  E4FF0BA5642EDCDD CRC64;
     MLDLTPQSKK ISIQIGGMTC QSCANRIEKV LNKKPFVQQA GVNFAAEEAQ VVFDATQASE
     AQIIEIIHKT GFSAHIKQAN ELPIEENTSI PWRLIVLWII NIPFLIGMLG MIGGSHNLML
     PPIWQFALAS IVQLWLAIPF YRGAIGSIRG GLTNMDVLVS TGTLTIYLYS AFMLFYHANH
     AMGHVYFEAS VMVIGFVSLG KFLEDRTKKH SLNSLSMLLQ LTPKKVTVLR NEKWIEIALD
     QVNIGEIIRA NQGERIAADG VIESGNGWCD ESHLTGESRP EEKQKGGKVL AGAMVTEGSI
     IYRANQLGSQ TLLGDMMNAL SDAQGSKAPI ARFADKVTSV FVPVVLVISL VTFALTYILT
     NDSVSSLIHA VSVLVIACPC ALGLATPAAI MVGLGKAVNA GVWFKDAAAM EETAHVDTVV
     LDKTGTLTKG ELEISALWQP QSAVYSEDDL YRFAAAVERQ ANHPIAKAIV QAAEXKMLEI
     PTALFSKMEV GQGIQAELEQ VGTIKVGKPD YCGLILPKNL EDIWQIASIV AVSINDEPIG
     AFALTDTLKN DSLHAIQRLQ QQNIDVVIMS GDQQSVVDYI AKQLGIKKAF GKLTPRDKAE
     QIQKLKDLGH IVAMVGDGIN DAPALASANV SFAMKSSSDI AEQTASATLM QHSVNQLVDA
     LFIARATLKN IKQNLFFALI YNILGIPLAA FGFLSPIIAG AAMALSSISV LMNALRLKKV
     RF
 
 
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