ID K9S7D5_9CYAN Unreviewed; 947 AA.
AC K9S7D5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:AFY66128.1};
DE Flags: Precursor;
GN ORFNames=GEI7407_1637 {ECO:0000313|EMBL:AFY66128.1};
OS Geitlerinema sp. PCC 7407.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC Geitlerinemataceae; Geitlerinema.
OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY66128.1, ECO:0000313|Proteomes:UP000010383};
RN [1] {ECO:0000313|EMBL:AFY66128.1, ECO:0000313|Proteomes:UP000010383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY66128.1,
RC ECO:0000313|Proteomes:UP000010383};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Geitlerinema sp. PCC 7407.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003591; AFY66128.1; -; Genomic_DNA.
DR RefSeq; WP_015171695.1; NC_019703.1.
DR AlphaFoldDB; K9S7D5; -.
DR STRING; 1173025.GEI7407_1637; -.
DR KEGG; gei:GEI7407_1637; -.
DR PATRIC; fig|1173025.3.peg.1835; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_3; -.
DR OrthoDB; 499468at2; -.
DR Proteomes; UP000010383; 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; 2.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000010383};
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 75..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 730..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..95
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 102884 MW; 1FC85EFE55AF4E46 CRC64;
MSSSLSSASA QASTPDLSQT PWYTLEPTKA LELLRSDREA GLSAEEVSQR QSIYGPNEIE
EGAGRSAWVI LFDQFKNIML LMLIVVAVVS AVLDVRSQQF PKDAVAIFMI VVLNGILGYL
QESRAEKALA ALKKLSSPKV RVIRGAQVVE VSSKELVPGD LMLLEAGSQV SADGLLLEAV
NLQVRESALT GEAHSVDKDA SQQMEEGAPL GDRLNMVFQG TEVVQGRATV LVTATAMETE
LGRIASMLQG VENEPTPLQK RMSQLGNVLV TGSLVLVTLV VAGGVAVGGW DRFEDLLEVS
LSMAVAVVPE GLPAVITVTL AIGTQRMVQR QALIRRLPAV ETLGSVTTIC SDKTGTLTQN
KMVVQRLQAG QENIRVTGEG YAPQGEFFDA QDQAIASDDQ PALQTLLLGS LLCNDALLQH
EQDHWVIIGD PTEGALLSLA GKAGFEQEVW KKKLPRVAEV PFSSDRKRMS VVCQREASDQ
LTIPGTDGAT YYVFAKGSPE LLMERCDRVL VGDRLEPITD DHRSATLDGN NDMASRGLRV
LGFAYRPLTE LPAEDAMEQV EESLVWLGLV GMLDAPRPEA RDAVERCRQA GIRPVMITGD
HRLTAQAIAH DLKIAQPSDR VLEGHELEKM SVEDLESQVD HVSVYARVSP KHKLQIVQAL
QRRGKFVAMT GDGVNDAPAL KQADIGIAMG ITGTDVSKEA SDMILLDDNF ATIVAATEEG
RVVYTNIRRF IKYILGSNIG EVLTIAAAPI LLPMGGVPLT PLQILWMNLV TDGLPALALA
VEPPEPDVMK RPPNSPNESI FARGLGSYMV RIGIIFAILT IALMLWAYNY SNAVTSDLLR
PERWKTMVFT TLCIAQMGHA IAVRSNSRLT VEMNPVSNPF VLGAVILTTL LQLSLVYVEP
LRNFFGTHYI SGLELLVCIG FSSLMFVWIE MEKLAIRLYH RARSSGG
//
