ID R5EBJ5_9CLOT Unreviewed; 871 AA.
AC R5EBJ5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=ATPase P-type (Transporting) HAD superfamily subfamily IC {ECO:0000313|EMBL:CCX88609.1};
GN ORFNames=BN724_01924 {ECO:0000313|EMBL:CCX88609.1};
OS Clostridium sp. CAG:590.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262825 {ECO:0000313|EMBL:CCX88609.1, ECO:0000313|Proteomes:UP000017939};
RN [1] {ECO:0000313|EMBL:CCX88609.1, ECO:0000313|Proteomes:UP000017939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:590 {ECO:0000313|Proteomes:UP000017939};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCX88609.1}.
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DR EMBL; CAXF010000155; CCX88609.1; -; Genomic_DNA.
DR AlphaFoldDB; R5EBJ5; -.
DR STRING; 1262825.BN724_01924; -.
DR Proteomes; UP000017939; 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 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; 2.
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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000017939};
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 59..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..768
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..868
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 871 AA; 94874 MW; 495488606DEC6D14 CRC64;
MKQVYQMDVD KVFTQMQTNE KGLSMQRAKE LLEEKGENVL EEGKKKTAVM VFLEQFKDLL
VMILIIAAIV SAVSGNAEST VVIFVVIILN AILGTVQYMK AEKSLNALKA LSMPYAKVIR
DGKKMEIPST EVVPGDIVIL EAGDMIVADG RIFNNYSLQV NESALTGEST NVDKVDYRLE
EDLPLADRRN MVYSGTLVTY GRAEVVVTGT GMETEMGKIA ELMNQAKEKK TPLQNSMDAF
SKRLATIIIV ICIVVFGLQL HQGTSFLNAL MFAVALAVAA IPEALTSIIT IVQAMGTQKM
AAEGAIIKQL KAVESLGCVS VICSDKTGTL TQNKMTVTDV YTEGQILKPE ELDLRNSTHR
YLLYNAVLNN DSSLQGEKGI GDPTESCLLV MARKAFAGGT LNFEEEDIRR MMPRLGEIPF
DSERKMMSSQ YMVHGTDTVF TKGALDVLMP KITRIRVNGT VQMISDKQKN DILACNEHFS
CNGLRVLAFV YKEVGEKETL CSDYENDYIF VGLTAMIDPP RPESVKAVSD AKRAGIKTVM
ITGDHKVTAT AIAKQIGIYE EGDYAVTGAE LDVMTQEELQ QKLKQISVYA RVSPENKIRI
VEAWQEQGEV VAMTGDGVND APALKKADVG VAMGVTGTEV SKDAAAMILS DDNFATIIKA
VENGRSVYRN IQNAIQFLLS GNMAGILCVL YCCVAALPAP FAPVHLLFIN LLTDSLPALA
IGTEKSDRGL LAEQPRDTKE GILTGNFIFH LFGYGMMIAI VTMTAFYIGL QSDAMTASTM
AFATLTLARL FHGFNCRGKK MIFRLGLFTN KWSIAAFLAG VGLLGIVLWM PALSGVFEVS
ALSIAQAGMI ALLAAVPTLC IQVTRTILGR E
//
