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
//