ID F4LVI5_TEPAE Unreviewed; 898 AA.
AC F4LVI5; L0S339;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN Name=yloB {ECO:0000313|EMBL:CCP26293.1};
GN OrderedLocusNames=TEPIRE1_1537 {ECO:0000313|EMBL:CCP26293.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP26293.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HF563609; CCP26293.1; -; Genomic_DNA.
DR RefSeq; WP_013778494.1; NC_019954.2.
DR AlphaFoldDB; F4LVI5; -.
DR STRING; 1209989.TepRe1_1425; -.
DR KEGG; tae:TepiRe1_1537; -.
DR KEGG; tep:TepRe1_1425; -.
DR PATRIC; fig|1209989.3.peg.1746; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_1_1_9; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000010802; 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:UniProtKB-EC.
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; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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 Hydrolase {ECO:0000313|EMBL:CCP26293.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802};
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 62..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..79
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 898 AA; 98551 MW; A13C58316AFA2B9B CRC64;
MEKINWYSLE KEDISGKLNT DLKNGLPSDL VEKRLESIGY NELVGKKGVT IWQMLLEQFK
DFLVLILIGA SFVSAIIGEV TDAVVIILIV ILNAVLGVMQ EFRANKALEA LKEMAAPEAK
VIRDGKIIEI PSRELVPGDL VLLEAGNYVP ADIRLVESVN LKIEEASLTG ESVPAEKNAE
VVLGGEVPLG DRSNSAFMGT VVTYGRGKGI VVATGMNTEI GLIAEMLESY EEGETPLQKK
LDELGKILGI ASLAICGIVF LLGIFRGIPI LEMFMTSVSL AVAAIPEGLP AIVTIVLALG
MQRMVQKHAI IKKLHAVETL GSTTVICSDK TGTLTQNEMT ARKVFVSNKV YSISGEGYKP
HGDFSIGDSK CEPLADTDLK MLLTIGLLCN DAKLEESSYG DEKTWRIIGD PTEGCLVVAA
TKAGLDTDEL CNRMPRLQEI PFDSERKRMT TFHSYEQKYV AFTKGAPDIM LNLSSKILKN
GKIFDINDED RKQILEVNHN MASQALRVLA FAFKPINDIP KKPDPVEIEK DMVFVGLIGM
IDPARPEAKD AIRICKEAGI RPVMITGDYK DTAEAIAREL GMIDENSKAL TGTELDMMDE
QQLAAAAKEV SVYARVSPIH KLRIVDAIKQ NGHIVAMTGD GVNDAPALKK ADIGIAMGIT
GTDVAKEAAD MILTDDNFAS IVSAVEEGRV IYSNIRKFIF FLLSCNIAEI LIIFVAMLFG
LPVPLKPIQL LWLNLLTDAF PALALGMEAK EPNIMKRPPR NPDEPILDRQ MNWQIAIQST
FMTIAVLGVF VFSLNNTSNL EIARTYAFAT LIFSELLRAY TSRSETLSVF KIGFFSNKFM
VGGTLVSFLL LLVVLYVPAL RYIFDTVKLS IYDWDIIVLF GIMPFLAAEI GKMFLKSK
//
