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Database: UniProt
Entry: S5SUK0_9CORY
LinkDB: S5SUK0_9CORY
Original site: S5SUK0_9CORY 
ID   S5SUK0_9CORY            Unreviewed;       899 AA.
AC   S5SUK0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Cation-transporting ATPase {ECO:0000313|EMBL:AGS34869.1};
GN   ORFNames=B841_06980 {ECO:0000313|EMBL:AGS34869.1};
OS   Corynebacterium maris DSM 45190.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS34869.1, ECO:0000313|Proteomes:UP000015388};
RN   [1] {ECO:0000313|EMBL:AGS34869.1, ECO:0000313|Proteomes:UP000015388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT   45190).";
RL   Submitted (NOV-2012) 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; CP003924; AGS34869.1; -; Genomic_DNA.
DR   RefSeq; WP_020934802.1; NC_021915.1.
DR   AlphaFoldDB; S5SUK0; -.
DR   STRING; 1224163.B841_06980; -.
DR   KEGG; cmd:B841_06980; -.
DR   PATRIC; fig|1224163.3.peg.1402; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_3_11; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000015388; Chromosome.
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   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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000015388};
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..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        691..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        724..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        764..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        795..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        833..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        865..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..84
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   899 AA;  95314 MW;  6E00D4EBAB7405E9 CRC64;
     MSTTAGAPVP DAHALPVDQV LDRLGSSVKG LSAGAVADRL AEHGPNALPQ AEQETWWQRL
     LRQFNDPMIY VLITAGVLTA IMGQVIDTAV IAAVVVINGL VGFIQEGKAA DALESIRDML
     SPESEVLRDG TWVQVPSEEL VPGDVVKLRA GDKIPADLRL LEAASLRTEE SALTGESLTA
     EKSLAAVDEA AGVGDRPSMV FSGTTVAAGS GVGVVAVTGA GTEIGRITGM IQDVEQVETP
     LTKAMGKFSS IIAVIALVLA VLMVLVSWLL YRTGWADLLM SAIGFAVAAI PEGLPAVMAI
     TLALGVQKMA GQNAITRRMN SVETLGSVTT ICSDKTGTLT RNEMTVQHVL TRAHTYQVSG
     VGYAPEGSVA VDGEPAALAE HRDLALIAEV AAYANDSAVR QTEDGAWKLA GEPTDGGIKV
     FALKTGCEDN GSRLATVPFD SEHKYMATLD DLDGDVFLHL KGAPDRLLDR SSAQISADGS
     TEPLDRAFWE DAVDELGGHG LRVLAAARRD ATHADRVSNA DVDEGEFTFI GLYGIIDPPR
     EEAIEAVRIV QDAGIRVRMI TGDHASTATA IAKEVGIADG RTITGPELES ASDEDLQRIV
     ADTTVYARTS PEHKLRLVQA LQRNGEVVAM TGDGVNDAPS LKQADVGVAM GVKGTEATKD
     AADIVLADDN FATISRAVSM GRNIYDNLKK AIVFMLPTNG AQGLVIFVAM LLGMTLPITP
     LQVLWVNLIT AVTLSLALSF EPAEPDIMKR KPRDPDASFL DSEAILRILY VSLLLGGATT
     LVFEWAISAG AQLDVARTWA VNTLVMGQVF YLFTARFSRV SALRKELFTT NPISWLCVGA
     MLVLQLAFVY LPFAQVAFQT TAVSLQSWLL SVTVGAVIFA AVEVDKALRR GAETRRATV
//
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