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Entry: G2ZCI7_LISIP
LinkDB: G2ZCI7_LISIP
Original site: G2ZCI7_LISIP 
ID   G2ZCI7_LISIP            Unreviewed;       626 AA.
AC   G2ZCI7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Putative heavy metal-transporting ATPase {ECO:0000313|EMBL:CBW85065.1};
GN   OrderedLocusNames=LIV_0587 {ECO:0000313|EMBL:CBW85065.1};
OS   Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW85065.1, ECO:0000313|Proteomes:UP000001286};
RN   [1] {ECO:0000313|EMBL:CBW85065.1, ECO:0000313|Proteomes:UP000001286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX   PubMed=22072644; DOI=10.1128/JB.06120-11;
RA   Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA   Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA   Goebel W., Glaser P.;
RT   "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT   provides insights into host specificities and evolution of the genus
RT   Listeria.";
RL   J. Bacteriol. 193:6787-6788(2011).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC       ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; FR687253; CBW85065.1; -; Genomic_DNA.
DR   RefSeq; WP_014092095.1; NC_016011.1.
DR   AlphaFoldDB; G2ZCI7; -.
DR   GeneID; 57075577; -.
DR   KEGG; liv:LIV_0587; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_3_9; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000001286; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07551; P-type_ATPase_HM_ZosA_PfeT-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43079:SF1; CADMIUM_ZINC-TRANSPORTING ATPASE HMA1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43079; PROBABLE CADMIUM/ZINC-TRANSPORTING ATPASE HMA1; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        89..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        239..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        266..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        577..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        602..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   626 AA;  67891 MW;  F11150730969F445 CRC64;
     MRNWMERNWQ FVTTGISGIL IIIGCIVGSE VGNFWTAVIF LSAFIIGGFE QAKEGIQATI
     KTKKLNVELL MILAATGASI IGYWFEGAVL IFIFSISGAL ETYTTNKSKR EITKLMAFQP
     EKAFRLLPNG DMEEVAAKDL QLEDMVIVRP GESVPIDGVI VRGSTTLNEA TINGESVPAM
     KTVGAEVFGG TVNVSSAITV KVTQTFDNTI FSKIIRLVET AQNEPSKTAR FIERFEDTYV
     KAVLLFVLVM MFLPHFVLGW SWNETFYRAM VLLTVASPCA LVASVTPATL AAISNGARHG
     ILFKGGVHLE NLRGVKAIAF DKTGTLTNGT PRLTDQLFKA NLNEKRIINV VVAMERQSLH
     PLAAALTKEL EAEVTENLVE IEVIDVPGWG VKAIYEGETW QIGKAGFVGG EAAKQFSGEV
     SEKLATEGKT IVYVAVDSEV IAMFALKDTC RQEAIQAVQA LKSKGIKTIM VTGDNQQTGE
     AIQTELGMDY VVAGCLPEKK VDVIKELSVT YGSVAMVGDG INDAPALAHA AVGIAMGEGT
     DIAMETADVV LMKNDLEKIA YAYTLSERLH RISWQNICFA ITVIVSLIAA NVFQLINLPF
     GVVGHEGSTI LVILNGLRLL KNNRKL
//
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