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Database: UniProt
Entry: A3CM87_STRSV
LinkDB: A3CM87_STRSV
Original site: A3CM87_STRSV 
ID   A3CM87_STRSV            Unreviewed;       922 AA.
AC   A3CM87;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Cation-transporting ATPase, E1-E 2 family, putative {ECO:0000313|EMBL:ABN44292.1};
DE            EC=3.6.1.- {ECO:0000313|EMBL:ABN44292.1};
DE            EC=3.6.3.10 {ECO:0000313|EMBL:ABN44292.1};
DE            EC=3.6.3.8 {ECO:0000313|EMBL:ABN44292.1};
GN   Name=pacL {ECO:0000313|EMBL:ABN44292.1};
GN   OrderedLocusNames=SSA_0866 {ECO:0000313|EMBL:ABN44292.1};
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN44292.1, ECO:0000313|Proteomes:UP000002148};
RN   [1] {ECO:0000313|EMBL:ABN44292.1, ECO:0000313|Proteomes:UP000002148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36 {ECO:0000313|EMBL:ABN44292.1,
RC   ECO:0000313|Proteomes:UP000002148};
RX   PubMed=17277061; DOI=10.1128/JB.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000387; ABN44292.1; -; Genomic_DNA.
DR   RefSeq; YP_001034842.1; NC_009009.1.
DR   AlphaFoldDB; A3CM87; -.
DR   STRING; 388919.SSA_0866; -.
DR   KEGG; ssa:SSA_0866; -.
DR   PATRIC; fig|388919.9.peg.827; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_3_9; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000002148; Chromosome.
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: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; PF12710; HAD; 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:ABN44292.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002148};
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        86..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        710..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        738..757
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        777..803
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        815..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        857..877
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        889..911
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..106
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  99622 MW;  09A9DF544F038FBD CRC64;
     MRLEMISRSG QKSSEIKEAK RRNTLSKEQK RQAFYTQSPE EIFKTLDASE QGLSSQEAAK
     RLADYGRNEL DEGEKKSLLM KFLEQFKDLM IIILLVAAVL SVVTSGGEDI ADALIILAVV
     IINAIFGVYQ EGKAEEAIAA LKSMSSPAAR VLRDGHVTEV DSKDLVPGDI VRLEAGDVVP
     ADMRLLEANS LKIEEAALTG ESVPVEKDLT VEVAADAGIG DRVNMAFQNS NVTYGRGVGL
     VVNTGMYTEV GHIAGMLQDA DETDTPLKQN LNSLSKVLTY AILVIAAVTF VVGVFIQGKN
     PLDELMTSVA LAVAAIPEGL PAIVTIVLAL GTQVLAKRNS IVRKLPAVET LGSTEIIASD
     KTGTLTMNKM TVEKVFYDGV LNEAGQDIEL GLELPLLRSV VLANDTKIDQ EGKLIGDPTE
     TAFIQYALDK GYDVKAFLEK YPRVAELPFD SDRKLMSTVH PLPDGKFLVA VKGAPDQLLK
     RCVARDKAGD VAAIDDATSQ LIKSNNSDMA HQALRVLAGA YKIIDAVPTD LTSENLENDL
     IFTGLIGMID PERAEAAEAV RVAKEAGIRP IMITGDHQDT AEAIAKRLGI IEEGDTEDHV
     LTGAELNELS DSEFEKVVGQ YSVYARVSPE HKVRIVKAWQ NQGKVVAMTG DGVNDAPALK
     TADIGIGMGI TGTEVSKGAS DMILADDNFA TIIVAVEEGR KVFSNIQKTI QYLLSANTAE
     VLTIFLATLF GWDVLQPVHL LWINLVTDTF PAIALGVEPA EPGVMSHKPR GRKSSFFSGG
     VMSSIIYQGV LQGALVLAVY GYAISNPVHV GDIKAIHADA LTMAFATLGL IQLFHAYNVK
     SVYQSIFTVG PFKSKTFNWS ILVSFILLIS TIVIDPLEKI FHVTKLDLSQ WTVVLIGSFA
     MIVIVEIVKF IQRKLGMDKN AI
//
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