ID C6PU11_9CLOT Unreviewed; 865 AA.
AC C6PU11;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=E1-E2 ATPase-associated domain protein {ECO:0000313|EMBL:EET87310.1};
GN ORFNames=CcarbDRAFT_2278 {ECO:0000313|EMBL:EET87310.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET87310.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET87310.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET87310.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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:EET87310.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACVI01000033; EET87310.1; -; Genomic_DNA.
DR RefSeq; WP_007061163.1; NZ_CP011803.1.
DR AlphaFoldDB; C6PU11; -.
DR STRING; 536227.Ccar_23545; -.
DR KEGG; cck:Ccar_23545; -.
DR PATRIC; fig|536227.13.peg.4861; -.
DR eggNOG; COG0474; Bacteria.
DR OrthoDB; 1937481at2; -.
DR Proteomes; UP000004198; 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 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; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
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 NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
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.
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:UP000004198};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 838..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 865 AA; 98116 MW; 87332B10B4AD9DD5 CRC64;
MIEWYDKPWS EVVKNFGSNI YSGLDEEQVK PHRDKYGANK IKMPRPPKLG KLIKNQIKNF
WMIILILVSI VFVYLHQYIS ASIGFFIIII NFLFVVLSEY NQGKSLKTLQ RLNMGNARVV
REGRTLKVPA EQLVVGDIVI VGKGEVIQAD LRVIESDELK TNESAVTGKS FIAEKYETKI
IDKELKLSDM KNILFKSSYV VDGSGTGIVI ATGMNTQISN IIKLFLGEKE EGKSFNERLN
GILNLFALFI LTPLVAILCI DFMQKENIKY ILKFSSTMIL NSTPQTIIVI VSIVSAILLK
IAKKQFIVFK NLSVMEKLAQ VSVICTDKVG AFSTNKMKVA KIYSDEVLID ALGSELRQGI
SEDKDVNIYR MTNIALLCND TKSIAGKLQN PKDDLMEIAL VKFARENGID KRDLERTHKR
IKQISFDTER RMMTTLNVVD ENCRANVKGA VDSILARCTY IMKDGLEVEI TDEDIEKIKQ
ADIEMSSECL SVIATAYRNF IYEPSLNENI ESHLVFSGLF GFENTIREDA IEAIEKSEFL
NIKPIIITED NKLTALALGK KLGTISNIQQ ILSGVEMDNM LDEEFKRIGD KINIFSRIDS
RHKVKIIRDL KEYGYTTAIT GSKLTDLPAL RVSDVGITTS SSNIVKKLSD IFVNDINFLQ
ILNSIEDSRK IISLIKKIIL YVVTNSTAMI TFTSIMHLYK REVPFILEEG LIFSCIAMTL
SCIAITYQYK NEKNECDGYI IDKTIIKDNM SFIIFNGVLM GAAASLAFQF GYSKGVMFAQ
ALSFGILNLN TVIFTYSFSN KLFFKNKLSN FIVFINFIIQ WCVLYLISGK NIIFNMEYLR
IIGIVIVIWF IICLFKKFDK EEIYD
//
