ID Q4FRP3_PSYA2 Unreviewed; 950 AA.
AC Q4FRP3;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE SubName: Full=Heavy metal efflux P-type ATPase {ECO:0000313|EMBL:AAZ19315.1};
GN OrderedLocusNames=Psyc_1467 {ECO:0000313|EMBL:AAZ19315.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ19315.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ19315.1, ECO:0000313|Proteomes:UP000000546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC {ECO:0000313|Proteomes:UP000000546};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19315.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4FRP3; -.
DR STRING; 259536.Psyc_1467; -.
DR KEGG; par:Psyc_1467; -.
DR eggNOG; COG2217; Bacteria.
DR eggNOG; COG2608; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR Proteomes; UP000000546; 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; cd02079; P-type_ATPase_HM; 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; IPR021993; ATPase-cat-bd.
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 NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 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 {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000546};
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 210..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 245..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 282..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 552..574
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 580..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 905..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 927..945
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 125..191
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 347..399
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 950 AA; 103958 MW; C7A91AF5D1336CF9 CRC64;
MSSIPSPMPP TSPTLPRSSS TNAYYHDNSI TEGLVLPLAG HCFHCGDPVP QPPFHSDILG
KSREMCCMGC QLASQSIVEA GLEQYYLDRS EINRTASLPT QMTRLEAYDH DEIKSQFVYA
QDGMSVAELS VNNLRCAACT WLIESRLDEL DGIDRCQVNL TNQRMRVIWD ESKLPISRIL
AVINEIGYEA KPYRQDTHEA MLARHNNQML IRLGIAALGS MQAMMYAVAI YFGEYSDMLI
FQRDFLRWVS LFVSTPVFFY AGVPFFTSAW SAIRARQVNM DVPVSIALII TFFASLYATI
TGQGETYYDS VSMFIFFLLA GRYIEHNARL KAATMANDLV VVEPVLVQKI AKDKKAAESI
LQLLEQNSSP KTAFVHSDLD EEDKDVANQE SQLATSEINN QSVKSTMPNF MQSMDAEVYQ
LTSRIAKEWQ QTRNQLLAVS NTNDEAKEKQ MVTAHSLQVG DIIMVEAGSE IISDGILLSP
TATVSQSLLT GEGDLISKTQ GDYIVGGAQN DSQPFEMLVT ALPEDSQIGL IDRLMNRAMS
EKPKLAQQAD KLARWFVARI LVLSVLVFIS WYIVDPSQAI WATVAVLVAT CPCALSLATP
IALTVSTNRL ASYGFLTTRG HTLQTLAEIT HVAFDKTGTL TYGKPNLLNI ELLIDTADIT
EAHEQRDDVL AIAAALEVGS RHPIAHALLT AAYQLHLPAT QALQHYPAGG VEAMIDGVLY
RIGHVDFALD KTNSDNISND LVIDLVGARA SSAVVLSCQK DESITWQALA CFYFNDKVRD
SAQSMLDSLK ALSIEPVMLT GDPSPQALVM AENLGMQSAY NGLSPMDKVN HIQQLQAQGA
VVLMVGDGIN DAPVLAAADV STSIAGAADL AQVSSDSIIL NGQIEAIIAA KRIADKTKRI
IKQNLRWALI YNGSILIPAA LGYVPPWLAA IGMSLSSLFV VLNALRLKRA
//
