ID A0A0R0A512_9GAMM Unreviewed; 733 AA.
AC A0A0R0A512;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KRG36215.1};
GN ORFNames=AK824_03200 {ECO:0000313|EMBL:KRG36192.1}, AK824_03350
GN {ECO:0000313|EMBL:KRG36215.1};
OS Psychrobacter sp. P11G3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1699623 {ECO:0000313|EMBL:KRG36215.1, ECO:0000313|Proteomes:UP000051518};
RN [1] {ECO:0000313|EMBL:KRG36215.1, ECO:0000313|Proteomes:UP000051518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P11G3 {ECO:0000313|EMBL:KRG36215.1,
RC ECO:0000313|Proteomes:UP000051518};
RA Ruckert C., Albersmeier A., Moghadam M.S., Winkler A., Lale R.,
RA Kalinowski J.;
RT "High quality draft genome sequence of Psychrobacter sp. P11G3, isolated
RT from an ascidian tunicate in the Norwegian sea.";
RL Submitted (AUG-2015) 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:KRG36215.1}.
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DR EMBL; LJCF01000001; KRG36192.1; -; Genomic_DNA.
DR EMBL; LJCF01000001; KRG36215.1; -; Genomic_DNA.
DR RefSeq; WP_057758752.1; NZ_CM003596.1.
DR AlphaFoldDB; A0A0R0A512; -.
DR STRING; 1699623.AK824_03200; -.
DR PATRIC; fig|1699623.3.peg.667; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000051518; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd07546; P-type_ATPase_Pb_Zn_Cd2-like; 1.
DR Gene3D; 3.30.70.100; -; 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; 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; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
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; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
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 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 98..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 356..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 674..699
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 733 AA; 76896 MW; 963855ABC42B55BD CRC64;
MKYHIEGMDC ASCIGKIETA LKRMPGVSDV QLNFATETLE LNLAPGAPTQ ASDIEKTIKS
LGFGISANTG QQTVSAIDID SDNQMAPQDK QWWQTQKGKQ VVGLGILMGS AYALSLLLPA
YGIWVFAIAV IVGVFPFARK ALALAKTGSF FSIETLMSVA VLGALIIGEA EEAAAVVFLF
SIGELFESIA ADRARAGIRA LSSLVPKSAI LLDAQGGQRN VPATSLQVND LVLVRPGDRV
SADGSIVQGA SSLDDSPVTG ESVPVAKTMG DNVFAGSINI DGVLQVRVEK TAADNTISRI
IELVEQAQAS KAPTARFIEK FSRYYTPAVM AIAALIIIIP PLAMGGDWST WLYRGLALLL
IACPCALVLS TPAAIASGLA VGARRGLLIK GGSALETIGQ VKTVAFDKTG TLTEGKPCVT
DVVAFTQEDS SIQGQNSQGQ DEILALFASV EIGSSHPLAE AIVSHAEAAK VVIPVASNAS
ATAGKAVHAT VAERALAIGS PVYAADEALI SFTQQAQIEA LQNEGKTVSV LFDEQNREVL
GLIALRDELR DDAHEGVAQL KAMGLRSVML TGDNRLTAQA LASNLDVEWE AELLPEDKLR
LLNEMKNNRK IAMVGDGIND APALATADVG IAMGGGTDVA IETADIALLK SRVTDMAHLI
ALSRATMRNI HQNVIFALGL KGVFLITTVF GITGLWIAVL ADAGATVLVT LNALRLLRFK
GAPPLVNPPK VVK
//
