ID H1FZY5_9GAMM Unreviewed; 912 AA.
AC H1FZY5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=P-type HAD superfamily ATPase {ECO:0000313|EMBL:EHQ51122.1};
GN ORFNames=ECTPHS_00435 {ECO:0000313|EMBL:EHQ51122.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51122.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ51122.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51122.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-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:EHQ51122.1}.
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DR EMBL; AGBG01000001; EHQ51122.1; -; Genomic_DNA.
DR RefSeq; WP_008930689.1; NZ_AGBG01000001.1.
DR AlphaFoldDB; H1FZY5; -.
DR STRING; 519989.ECTPHS_00435; -.
DR PATRIC; fig|519989.5.peg.89; -.
DR eggNOG; COG0474; Bacteria.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000005314; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02080; P-type_ATPase_cation; 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; 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 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 699..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 803..822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..86
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 98754 MW; 1CEBA63B8DF8E5F0 CRC64;
MSEEKETEVT PRWHHLEAGD AIGQLETSDR EGLTTDEIER RRAEYGPNRL PPPKTRGPLG
RFLAQFNNLL IYVLLGAAVI TALLGHWVDT GVILAVVLLN SIIGFVQEGK AEKALQAIRD
MLSPHAAVIR GGERMTVEAE ALVPGDLVLL ESGDKVPADL RLIKVKGLQV QEAMLTGESV
PVDKSVEAVS AEADLGDQTS MAFSGTLVTA GQATGVVVET GARTQIGRIS TLLSDVESLT
TPLLRAMNVF ARWLTVAIIG LAGLVFAFGM LVWDYTAVEM FMASVALAVA AIPEGLPAIL
TVTLAIGVQF MASRNAIIRR LPAVETLGSV SIICSDKTGT LTRNEMTVRS VALAGRDYEI
TGVGYDPHGG FTVDGKEVDP AGEDLLLEAL RAMVLCNDSR LRKKDGQWQV EGDPMEGALL
TAGIKAAMDP VFEHKDRPRT DIIPFESEHR FMATLNHDHE GQGMIYVKGA PEQLLEMCCR
VRTTDGPAAL DRDAWLERVD ALAARGERVL AVACMPADPG HRELKFSDVE DGLELIGLFG
LIDPPREEAI QAVADCQQAG IRVKMITGDH AGTARAIAGQ LGLANGDKVL TGRDLDAMDD
ETLRRTVPEV DVFARTTPEH KLRLVRALQW HGYVVAMTGD GVNDAPALKQ ADVGVAMGRN
GTETAKEASE MVLADDNFAS IAHAVREGRR VYDNLKKAIT FLLPINSGES GSIVAAIMLG
MALPITPLQV LWVNMVSSVA LAMALAFEPA EKNVMKRPPR APGEAILSLF LIWRILFVSF
LFLIGIFGIY LWSVQQGYSV EMARTHAVNT LVVMEIFYLL SVRSLQVTSL SFKGLIGTRA
VLIAILIVVA LQLMFTYAPF MQFFFDSEPV GLKEWGVILA VGVVLFFILE LEKAVRNRIN
NESGRRTGAV GS
//
