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Database: UniProt
Entry: D9SMG4_CLOC7
LinkDB: D9SMG4_CLOC7
Original site: D9SMG4_CLOC7 
ID   D9SMG4_CLOC7            Unreviewed;       867 AA.
AC   D9SMG4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:ADL53820.1};
GN   OrderedLocusNames=Clocel_4159 {ECO:0000313|EMBL:ADL53820.1};
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL53820.1, ECO:0000313|Proteomes:UP000002730};
RN   [1] {ECO:0000313|EMBL:ADL53820.1, ECO:0000313|Proteomes:UP000002730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC   {ECO:0000313|Proteomes:UP000002730};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP002160; ADL53820.1; -; Genomic_DNA.
DR   RefSeq; WP_010074175.1; NC_014393.1.
DR   AlphaFoldDB; D9SMG4; -.
DR   STRING; 573061.Clocel_4159; -.
DR   KEGG; ccb:Clocel_4159; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_2_9; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000002730; Chromosome.
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   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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002730};
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}.
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        670..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        742..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        808..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        842..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..76
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   867 AA;  95084 MW;  5BDB82B1A6DDFDC8 CRC64;
     MSEFYRKPKE EIMNILGVSD GGLNDEEVLK QRGKYGFNEL EEAKKKSAIQ IFFDQFKDFL
     VIILLVAATI SAFLGKLEST IVILIVVTIN AILGTIQHIK AEQSLNSLKA LSSPTAKVLR
     NGVKIEIPSR EILVGDILYL DAGDYVSADG RVIETYSLQI NESSLTGESE SVNKEIETID
     KDNITIGDRK NMVFSGSFVT YGRGVILVTD IGMKTEIGKI ANLLESTKEK KTPLQVSLDN
     FGKKLAIAII AISAVIFALD IFRGYPIIDS FMFAVALAVA AIPEALSSIV TIVLALGTQK
     LAKLNAIVRK LHAVESLGSI SVICSDKTGT LTQNKMTVKK VFVDDRIINH DNLQYHKEIE
     KKLVIMALLC NDAVTTENKE IGDPTEVALV NLGEEYNLDE LVVRKEHPRI AEIPFDSDRK
     LMSTVNKIDD KTLMITKGAL DVLLSRSTSI ETANGVKPLL EEHKKEIEDI NRQLSTDGLR
     VLAFASKDVE ENETINLDYE KDLCFIGLIA MMDPPREESK DAVANCISAG IKPVMITGDH
     KITASAIAKQ IGILKNESEA MEGFELEKIS DEELKSKVAE ISVYARVSPE HKIRIVRAWQ
     ERGNVVAMTG DGVNDAPALK QADIGIAMGI TGTEVAKDAA AMVLTDDNFS TIVKAISNGR
     SIYANIKNSI KFLLSGNTAG IISVIYASLT ALPVPFAPVH LLFINLLTDS LPAIAIGLEP
     HNQNIMKEKP RDINVPILNK EFAIEVALEG FLIALGTIIA FHIGLSTGDN VVASTMAFST
     LCLSRLFHGF NCRSKESIFR IGVFSNQFVW FSLIIGFLLL VAVLMINPLM QVFEVARLTL
     TQYGYICGLS VMPLVVVQLY KLIFIRK
//
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