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Database: UniProt
Entry: V2TS84_9GAMM
LinkDB: V2TS84_9GAMM
Original site: V2TS84_9GAMM 
ID   V2TS84_9GAMM            Unreviewed;       893 AA.
AC   V2TS84;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:ESK40462.1};
GN   ORFNames=P256_00915 {ECO:0000313|EMBL:ESK40462.1};
OS   Acinetobacter nectaris CIP 110549.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1392540 {ECO:0000313|EMBL:ESK40462.1, ECO:0000313|Proteomes:UP000023785};
RN   [1] {ECO:0000313|EMBL:ESK40462.1, ECO:0000313|Proteomes:UP000023785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110549 {ECO:0000313|EMBL:ESK40462.1,
RC   ECO:0000313|Proteomes:UP000023785};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA   Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter nectaris CIP 110549.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK40462.1}.
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DR   EMBL; AYER01000003; ESK40462.1; -; Genomic_DNA.
DR   AlphaFoldDB; V2TS84; -.
DR   STRING; 1392540.P256_00915; -.
DR   PATRIC; fig|1392540.3.peg.886; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_11_2_6; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000023785; Unassembled WGS sequence.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 3.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 3.
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; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   NCBIfam; TIGR00003; copper ion binding protein; 3.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 3.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 3.
DR   PROSITE; PS50846; HMA_2; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023785};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}.
FT   TRANSMEM        239..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        274..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        312..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        493..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        521..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        837..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        862..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          7..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          76..140
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          147..212
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   893 AA;  97174 MW;  C1FE8555133610D5 CRC64;
     MSAQEYERLE FTVHGMTCAS CVGRVEKVLH KQENIQDVNV NLATEKVAVL GRDLNKEKIV
     SIIERAGYEA IMPQTMQVIL HIEGMTCASC VGRVEKVLQK QQGVEAVSVN LATEKAVIEG
     VNLQPLVLLK AIEKAGYTAS QVNQKNKTLD LEIQGMTCAS CVGRVEKALR KVEGVKNVSV
     NLATESASVE TDEHIEPKLL VQIVEKAGYD AQLKIKNNEK DESLTVKREA EAQLFKQDLF
     IAFICTLPVF ILEMGTHLSM SFHKFVLTHI GQQLSWYIQF ILTTVVLVFP GRRFYKKGLP
     ALWRLAPDMN SLVALGTLAA YGFSCIATFL PNLLPQNTIN VYFEAAAVIV TLILLGRYLE
     AKAKGKTSQA IERLIGIQPK TARILQNGQL KEVDISDVHN GMIVVVQAGE KIAVDGLVID
     GHSFVDESMI TGEPIAVKKD KDSHVVAGTV NQQGILHIQV NATGNDTVLS QIIRLVEEAQ
     SSKLPIQSIV NKVTMWFVPV VIGLATLTFI AWLVFGPSPA FSFALVNAVA VLIIACPCAM
     GLATPTSIMV STGRGAEMGV LFRKGEALQT LKEAKVIAFD KTGTLTEGKP KLTDLDTIDH
     QNKDDVLQYM ASVEQYSEHP VAEAIVNHAK AQQIPLLNSS EVRVIAGYGI QAVVNEKSVY
     IGADRFMEKL DLDIKPFAVK AEQLAEDGKT PFYIAIENLV VAIVAVADDI KPSTYRAIQS
     LHELGLKVVM ISGDNYKTAR AIAQKLKIDD VIAEVLPQGK VDAIQKLQQT YGKVGYVGDG
     INDAPALATA DIGLAVGTGT DVAIESADVV LMSGNLQTVT QAIALSKATI RNIQQNLFWA
     FIYNIALIPI AAGALYPFYH ILLLPMISAF AMGLSSVFVL TNALRLKRFS YPI
//
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