ID A8M6X9_SALAI Unreviewed; 906 AA.
AC A8M6X9;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:ABW00347.1};
GN OrderedLocusNames=Sare_4579 {ECO:0000313|EMBL:ABW00347.1};
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=391037 {ECO:0000313|EMBL:ABW00347.1};
RN [1] {ECO:0000313|EMBL:ABW00347.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205 {ECO:0000313|EMBL:ABW00347.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000850; ABW00347.1; -; Genomic_DNA.
DR AlphaFoldDB; A8M6X9; -.
DR STRING; 391037.Sare_4579; -.
DR KEGG; saq:Sare_4579; -.
DR PATRIC; fig|391037.6.peg.4628; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_2_11; -.
DR OrthoDB; 9814270at2; -.
DR GO; GO:0005886; C:plasma 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 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; 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; PF08282; Hydrolase_3; 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 68..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..85
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 906 AA; 94813 MW; A6E9AA2BBFCCAB8E CRC64;
MTTSVLSGGP VHHGLPAHRV VLLLETDAHR GLGEREAGER LARHGPNTLP PAKGAGLLVR
ILRQFHHPLI YVLIAAGVIT AVLAEYVDSA VIFGVVLINA VVGFIQESKA EAALEGLRSM
AHTRATVIRD GHRRAVASED LVPGDLVLLE AGDKVPADMR LTRLAELRIN ESALTGESVP
VTKDEVVLPD GLPVADRRNM AYSGTLVTTG SGAGIVIATG AKTELGQIHR LVGSAQVLDT
PLTQKLAGFS KILTVAILAL AAVTFAVGLL RGHNAVETFT AAVALAVGAI PEGLPAAVTI
TLAIGVTRMA RRRAVIRRLP AVETLGSTTV ICSDKTGTLT ENQMTVRNLW TPAGLYEVTG
SGYAPDGALH SPTGKVTALK ADQALRWSLL AGAACNDAAL TCRDGHWDIV GDPTEGAMVV
VARKAGFTSD QVKATLPREA TIPFSSDRQY MATLHRDATK SPPGQVVLAK GGVERMLELC
GAQMDADGTI RGMDRDAVLE AAGQMAGRAL RVLATAMRPA PGADDFTVDR LPGSMVLTGL
QAMLDPPRAA ATAAVAACHT AGVKVKMITG DHAATAAAIA GQVGLLDPTQ SGTDMVLTGA
DLAALPAEEF PDAVDRAAVF ARVAPEQKLR LVEALQARGH VVAMTGDGVN DAPALRQAGV
GVAMGASGTE VAKDAADMVL TDDDFATVEA AVEEGRGVFD NLTKFITWTL PTNIGEGLVI
LAAILFGAAL PILPTQILWI NMTTAVALGL MLAFEPKETG IMTRPPRDPH QPLLTRALMA
RVLLVSTLLV AGSWWLFHWE LGNGASLAEA RTAAVNLFVV VEAFYLFSCR SLTHSAWRIG
LFTNRWLIAG VTVQALGQLA ITYLPAMNIL FSTAPIDGGA WLHILGIAAV ASLVVAVDKR
LRPAGR
//
