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Database: UniProt
Entry: A7GRK4_BACCN
LinkDB: A7GRK4_BACCN
Original site: A7GRK4_BACCN 
ID   A7GRK4_BACCN            Unreviewed;       907 AA.
AC   A7GRK4;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:ABS22762.1};
GN   OrderedLocusNames=Bcer98_2526 {ECO:0000313|EMBL:ABS22762.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS22762.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS22762.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000764; ABS22762.1; -; Genomic_DNA.
DR   RefSeq; WP_012094969.1; NC_009674.1.
DR   AlphaFoldDB; A7GRK4; -.
DR   STRING; 315749.Bcer98_2526; -.
DR   GeneID; 56418067; -.
DR   KEGG; bcy:Bcer98_2526; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_1_0_9; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR   CDD; cd02089; P-type_ATPase_Ca_prok; 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; 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; IPR005782; P-type_ATPase_IIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01116; ATPase-IIA1_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   Pfam; PF00702; Hydrolase; 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   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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:ARBA00022448}.
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        692..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        723..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        765..788
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        800..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        829..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        868..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..76
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   907 AA;  99333 MW;  0BA07EAFB984C453 CRC64;
     MNWYEMRAHE VEERTNTNVK TGLSEQEAEG RLKKFGPNEL QEAKRPSAFL VFLAQFKDFM
     VLVLFGATII SAFLGEYIDS IAIVAIVILN GILGFFQERK AEKSLEALKE LAAPQATVLR
     NGKWIKAPSK ALVLGDIIRF SSGDRIGADV RLVETSSLYI EESALTGESV PVQKKVEALS
     GQDVAIGDQK NIAFMGTMIT RGSGIGVVVA TGMNTAMGQI ANMLQNAEPM ETPLQRRLEQ
     LGKILIVVAL ILTALVVLAG VYQGNEVYHM FLAGVSLAVA AIPEGLPAIV TVALSLGVQR
     MIKKKAIVRK LPAVETLGCA SVICSDKTGT MTQNKMMVTH MWSGGELWKV TGKGYEPTGS
     FMKGEEKIDP ENTKSLYQLL TFGCLCNHAR IVKKKKEYVL DGDPTEGALV AVAMKAGISR
     EALKGNFEII HEFPFDSTRK MMSIIVRDRD GKKFVVTKGA PDVLLQKSQT ILWGNKQQPF
     SELYRKEVQA AIHSLGSQAL RTIAVAFKPL KVTDPIHDEQ EIEKDFMLVG IQGMIDPPRP
     EVKQAVQECK EAGIKTVMIT GDHKVTAMAI AEELGILPRN GRVIEGVELA NMTVDELEDI
     VEDTYVFARV SPEHKLKIVK ALQNKGHIVA MTGDGVNDAP AIKAADIGIS MGMTGTDVAK
     EASSLVLLDD NFATIKAAIK EGRNIYENIR KFIRYLLASN VGEILVMLFA MLLALPLPMV
     PIQILWVNLV TDGLPAMALG LDAPEGDVMK RNPRHPKEGV FARGLAWKIV SRGFLIGAVT
     LLAFIIAYNQ HPNELKYAQT VAFATLVLAQ LIHVFDCRSE HSVFHRNPFG NIYLVGAVIV
     SILLMLVVIY YPPLQPIFST LPIQARDWLL IVGLSSIPTF LLVGSLLTGN NEKKKKSLLY
     KKGLNLK
//
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