ID B0PA51_9FIRM Unreviewed; 887 AA.
AC B0PA51;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Putative potassium/sodium efflux P-type ATPase, fungal-type {ECO:0000313|EMBL:EDS11729.1};
GN ORFNames=ANACOL_01620 {ECO:0000313|EMBL:EDS11729.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS11729.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS11729.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS11729.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS11729.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS11729.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS11729.1}.
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DR EMBL; ABGD02000012; EDS11729.1; -; Genomic_DNA.
DR RefSeq; WP_006874916.1; NZ_DS544181.1.
DR AlphaFoldDB; B0PA51; -.
DR STRING; 169435.ERS852551_03355; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_0_9; -.
DR Proteomes; UP000003803; 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; 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 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 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..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 826..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..81
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 887 AA; 95875 MW; EAC3BFAE23A91A7E CRC64;
MDDHRRTPWH CQPVQEVYEA LRTSSEGLSD AEAAERLKKD GHNELRSKPP KTILQMLYSQ
LIDPMVLILV GAAVCSAVLR EWTEAGVIFA IVALNAVIGI VQEKKAQSSL EALRNMSAPT
ARVLRQGDES IIPASEVVAG DIVFLSDGDM VPADMRLIDS ANLKVQEASL TGESVPSEKD
ADDLLPLDCP LGDRSNMVYT SSIVTYGRAT GIVVATGMNT QVGGIAEMLE EQDELDTPLK
RKLNAVGKTL TIVGLIVCVM IFLIGALYQR PLIPQFLVAI SLAISIIPEG LPATATIVMA
LGVQRMAKRN ALVRNLPAVE TLGSATVICS DKTGTLTLNQ MTVTHIAVNG DFEAGATTPI
AEATGQHPIV YKELVYAAAL CNDASVDPDH AGAIIGDPTE GALIHMAQAF GVDHEALEDT
YPRRFEQPFD SDRKRMTTVH VISGNWISYT KGAVDEMLPL CTHILTADGV RPITEGDRAN
ILRLCLSMSE QALRVLGFAT RTLTGEQIPE EDGDNVEYDM TFLGVTGMID PPRKEVADSV
RTCRQAGIRT IMITGDHKVT ALAIARELDI YRPGDTVISG DELDELEDAA LDAAVKNATV
FARVSPADKL RIIQSLRRTG EVAAMTGDGV NDSPALKAAD IGVAMGITGT DVAKDAADMI
LLDDSFTTIA YAIKEGRRVY RNIQKVIQFL LAGNIAEITT LFAATIFNWE APLLAVHILW
VNLATATLPA LALGVDPASK NIMKHPPVKS GTLFEKDLVC RVITQGIFVA AMTTLAYWIG
ARMDNPTTGQ TMAFCVLAFS QMLRAFNQRS NTEPIWVRAE GINPWLVLSF LVSAALMACI
LLLPSPQSAF KLTGLSSVQW IAVLMLSLSS VLQIEVVKWF KRQKQHG
//
