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Database: UniProt
Entry: K6X9N4_9ALTE
LinkDB: K6X9N4_9ALTE
Original site: K6X9N4_9ALTE 
ID   K6X9N4_9ALTE            Unreviewed;       873 AA.
AC   K6X9N4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE            EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN   Name=ctpF {ECO:0000313|EMBL:GAC17309.1};
GN   ORFNames=GARC_0327 {ECO:0000313|EMBL:GAC17309.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC17309.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC17309.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC17309.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:GAC17309.1}.
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DR   EMBL; BAEO01000006; GAC17309.1; -; Genomic_DNA.
DR   RefSeq; WP_007616050.1; NZ_BAEO01000006.1.
DR   AlphaFoldDB; K6X9N4; -.
DR   STRING; 493475.GARC_0327; -.
DR   eggNOG; COG0474; Bacteria.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000006327; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        745..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        811..831
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        837..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..77
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   873 AA;  95510 MW;  92609D54E2FAA3A3 CRC64;
     MNKNYYQLDV ETALSELETS EIGLSCEQAQ IRLQKNGPNV IPSKKAQSIW QLFFRQFADF
     MIIVLLVAAL VSGVIGELID SLAILIILLL NAVVGTVQEF RAQRSLEALQ KMASPSASVL
     RDGQAVTLPE EKLVVGDIVL LEAGNIVPAD IRLIEVEELQ VNESSITGES QSVFKQQAEL
     KDNNLFIGDQ KNCVFKASMI TSGRASGVVF SSGLNTEIGK IANLLQQQDD TKTPLQIRLA
     KFGRYLASAI LFICAILLVI GLLQGQPLLL MFLTSVSLAV AAIPEALPAV ITISLALGAR
     KLLKQQALVR NLPAVETLGA VTYICTDKTG TLTVNKMSVE RVYIGQQQSS LLATDSVQLE
     QTLGQALAIS NDVIQKDGIP FGEPTELALF EFAKRSGFDK DQLIMDMPRE AVISFDSQRK
     LMTTLHSTST DVVAYVKGAA ESVLANCVKT QQEGDQIAID KTQILAEAEQ LANDGYRVLA
     LAKRSFDSMP EHLSAVTIEQ DLTFLGLVAL TDPLRTEVPQ AMADCISAGI TPVIITGDHR
     GTALAIAKRL HIANGEPKML DGDELDRISD QELKDNVCSI QLFSRVSPLQ KLKIVKALQE
     NNQFVAMTGD GVNDAPALQR ANIGIAMGQT GTDVARGASD MVLLDDDFST IVRSVKAGRR
     IFDNIRKFIK YTMSSNSGEI WTLFLAPFCG LPIPLLPIHI LWINLVTDGL PGLALSAEPA
     ERNIMQRPPR PVEESFFTHG MWQHILWVGL TVGGISIATL AWTIERNVNY WQTSVFTVLV
     FCQLFHSLAV RSESESIFTI GIFSNKPMFS SIALTVLLQL MVVYTPAFNH ILHTQPLPLD
     ALLICIAVSS IILWAVEGEK FLIRRGILYN KER
//
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