ID K8GHC9_9CYAN Unreviewed; 915 AA.
AC K8GHC9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=P-type ATPase, translocating {ECO:0000313|EMBL:EKQ66886.1};
GN ORFNames=OsccyDRAFT_4696 {ECO:0000313|EMBL:EKQ66886.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ66886.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ66886.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ66886.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ66886.1}.
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DR EMBL; AJUB01000019; EKQ66886.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GHC9; -.
DR STRING; 864702.OsccyDRAFT_4696; -.
DR PATRIC; fig|864702.5.peg.5043; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_0_3; -.
DR OrthoDB; 499468at2; -.
DR Proteomes; UP000001332; 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; 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; 3.
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; 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:UP000001332};
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 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..87
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 915 AA; 98436 MW; E698C18D406328E5 CRC64;
MQAIAPSNQS HPTYHELSNL EIIQYLATDA NQGLTHTEVT QRQHQYGLNE LATKPVKPAW
IRFLLQFNQS LLYILIIAGA IKAFLGSWTN AAVIWGVTVI NAVIGFVQES KAEGAIAALA
KVVTTEATVI RAGRKQVIPS SELVPGDLVL LTSGDKVPAD LRLLTVRGLQ VDESALTGES
VPVEKSTQPL PADTPLAERT NLAYAGSFVT FGQGTGIVIA TGNRTEVGQI SQSLDQRQHL
STPLTRKFAK FSQALLYIIL SLASFTFFVG LGRGKTWAEM FEAAVALAVS AIPEGLPAVV
TVTLAIGVNR MARRHAIIRK LPAVETLGGA TVICSDKTGT LTENQMTVQA IYAGGHLYHV
SGLGYAPEGK VCTEAGEAIA EDHATVIDLR RLPALQSCLI AGALCNDSHL EWQDHQWGLV
GDPTEGALIV AAQKAGLEQK QLNEWLPRLD SIPFESQFQY MATLHQGIDG HIIYMKGSLE
AVLNRCQAMR NVAGHAIPIE RKSLEIEAER LAEQGLRVLA FAEKLVPQHQ TTLDHIDLEG
GLTFLGLQGM IDPPREETIA AVSACQSAGI QVKMITGDHL TTATAIAKRI GLNKEGKLLG
FTGQQLAEMT DSDLSQAIES ASVFARVAPA QKLRLVETLQ AKGEIVAMTG DGVNDAPALK
QADIGIAMGK AGTDVAREAA DMLLTDDNFA SIEAAVEEGR TVYQNLRKAI AFILPVNGGE
SMTILISALL GRDLPILSLQ VLWLNMVNSV AMTVPLAFEP KSKRTMAQPP RNPKEPLLTG
KLLQRIAAVS VFNWVLIFGM FEWARQTTGN IAIARTMAIQ ALVAGRIIYL LSVSHLGTAI
ADRLRGRKTS FKDAAAIGIG MLGAIALQIV FSQWNVMNAL FATAPLTLYQ WVICLIPVLP
MIVLAIVVNR LDPTD
//
