ID A0A3S1A219_CHLFR Unreviewed; 1017 AA.
AC A0A3S1A219;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=PCC6912_19880 {ECO:0000313|EMBL:RUR83745.1};
OS Chlorogloeopsis fritschii PCC 6912.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR83745.1, ECO:0000313|Proteomes:UP000268857};
RN [1] {ECO:0000313|EMBL:RUR83745.1, ECO:0000313|Proteomes:UP000268857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR83745.1,
RC ECO:0000313|Proteomes:UP000268857};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
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:RUR83745.1}.
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DR EMBL; RSCJ01000006; RUR83745.1; -; Genomic_DNA.
DR RefSeq; WP_016877606.1; NZ_RSCJ01000006.1.
DR AlphaFoldDB; A0A3S1A219; -.
DR STRING; 211165.GCA_000317285_00014; -.
DR OrthoDB; 499468at2; -.
DR Proteomes; UP000268857; Unassembled WGS sequence.
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 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; 3.
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:UP000268857};
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 73..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..972
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..93
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 421..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 111422 MW; 0CF74F5A95321E19 CRC64;
MPSPITPSNS KSVSDMATAW HTIEIEESLL LLDSDRNVGL TNQQAIARLQ RYGHNELQEQ
SGRSSLSILI DQFTNIMLLM LMAVAVVSAI LDLRAAEFPK DAIAISAIVI LNGLLGFIQE
NRAEKALVAL KRLSSPKVRV IRDGRIIEVQ AKELVPGDVM LLEAGMQIAA DGRLLECQNL
QVREAALTGE ALAVSKREQM QLPTDVPLGD RINMVFQGTE VVQGRGKVLI TATGMQTELG
RIAKMLQSVE AEPTPMQQRM SQLAKALVTG SLIIVAVVVL GGILRTGSLR YFEEVLEVSL
SMAVAVVPEG LPAVITVTLA IGTQRMVRRH ALIRKLAAVE TLGSVTTICS DKTGTLTQNK
MVVQWVHSAS HSFKVTGDGY APIGTFELHQ FQSQIGIHTE QLPPPVDVLP NIFDSNENRS
NLLERQPLEA TSKTTDSLAG RGSKGTPQEV APKDINPDEY PELQTLLVAC VLCNDAVLDY
EQNQWEILGD PTEGALLSLA GKAGIEKTRL ERLFPRVAEF PFSSERKRMS VIVETDECVV
FSQQLNSASA EDSAYLMFTK GSPELVLGLC TSYQDGDSIP QTLHDGARAR ATECTQPLSD
RQRAHILEQN NQMASKGLRV LGLAYKPLKT LPSEGSEETI EQELIWLGLV GMLDAPRPEV
REAVRRCQEA GIRPVMITGD HQLTATAIAY DLGIAKQGDI VLNGQDLEKL ESVELEQQVN
YVSVYARVSP EHKLRIVQAL KKRGQLVAMT GDGVNDAPAL RRADIGIAMG ITGTDVSKEA
SDMVLLDDNF ATIVAAIEEG RVVYDNIRRF IKYILGSNVG EVLTVAAAPL LGLGGVPLSP
LQILWMNLVT DGLPALALAM EPAEPDVMRR PPYNPHESVF ARGLGLYIIR IGIIFAILTI
ALMAWAYNYT QNSGEPDRWK TIVFTSLCLA QMGHALAIRS NTQLTLQLNP FSNPYVLAAI
TLTTVLQLML IYVAPLRNFF DTHWLNSIEL AISIGFSALM FVWIELEKLF IKWFFTH
//
