ID Q8E025_STRA5 Unreviewed; 930 AA.
AC Q8E025;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Cation-transporting ATPase, E1-E2 family {ECO:0000313|EMBL:AAM99797.1};
GN OrderedLocusNames=SAG0911 {ECO:0000313|EMBL:AAM99797.1};
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAM99797.1, ECO:0000313|Proteomes:UP000000821};
RN [1] {ECO:0000313|EMBL:AAM99797.1, ECO:0000313|Proteomes:UP000000821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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DR EMBL; AE009948; AAM99797.1; -; Genomic_DNA.
DR RefSeq; NP_687925.1; NC_004116.1.
DR RefSeq; WP_000168898.1; NC_004116.1.
DR AlphaFoldDB; Q8E025; -.
DR STRING; 208435.SAG0911; -.
DR KEGG; sag:SAG0911; -.
DR PATRIC; fig|208435.3.peg.916; -.
DR HOGENOM; CLU_002360_3_3_9; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000000821; 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 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; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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; PR00121; NAKATPASE.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000821};
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 58..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 832..848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 900..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..86
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 930 AA; 102584 MW; 752F879CCC19A8D3 CRC64;
MASTNNVSDT NTRFAKEELE EVFEELGTTQ GGLSDEEVAV RQKKYGLNLL SEVKQESIIL
LFLKNFTSLM AILLWVGGFV AIVSNSLELG LAIWMVNVIN GIFSFIQEYR ASQATQALEK
MLPSYSRVLR KGSEEKILSE QLVPGDIVLI EEGDRISADG RLIKTTDLQV NQSALTGESN
PIYKDSNVEN DQSKTLIECD NMVFAGTTVS SGSATMVVTA IGMQTQFGQI ADLTQGMKSE
KSPLQRELDR LTKQISIISI TVGIIFFLAA TFFVKEPVSK SFIFALGMIV AFIPEGLLPT
VTLSLAMAVQ RMAKEHALVK KLSSVETLGA TSVICSDKTG TLTQNEMTVN HLWQNGKSYQ
VTGLGYAPEG QILFEGDNIC FGNSDRGDLE KLIRFAHLCS NAQVLPPNDD RSTYTVLGDP
TEACLNVLLE KSGINIQENR KFAPRLKELP FDSVRKRMTT IHSLGGDEKD KKISITKGAP
KEILDLSDYV LSDGKVIPLN KEERNKIQLA NDTFAKDGLR VLAVSYCDIE GFSKEQWTQE
NLEQHMVFIG LIAMSDPPRE GVREAIDKCH AASIRIIMVT GDYGLTALSI AKNIGIIRND
DAKVISGLEL SEMTDSQLKK ELSGEVVFAR VAPEQKYRVV TILQEMGEVV AVTGDGVNDA
PALKKSDIGV AMGVTGTDVA KESADMILTD DHFASIVHAV EEGRAVYQNI KKFLTYIFNS
NTPEAVPSAF FLFSKGFIPL PLTVMQILAV DLGTDMLPAL GLGVEPPETD VMNRPPRRLT
DRLLDKGLLI KSFLWYGTIE SVLAMGGFFW AHYLRYGNFT FFVANGIPYR EATTMTLGAI
IFSQIGMVMN SRTSYQSIKA LSIFGNKLIN FGIIMEILAF LVLVYVPLFH NLFNTASLGL
SHWLYLISCP FIMIGLDEVR KLFSSRKNKR
//
