ID G5J5B4_CROWT Unreviewed; 783 AA.
AC G5J5B4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Cation-transporting P-type ATPase {ECO:0000313|EMBL:EHJ12612.1};
GN ORFNames=CWATWH0003_2676 {ECO:0000313|EMBL:EHJ12612.1};
OS Crocosphaera watsonii WH 0003.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ12612.1, ECO:0000313|Proteomes:UP000003477};
RN [1] {ECO:0000313|EMBL:EHJ12612.1, ECO:0000313|Proteomes:UP000003477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ12612.1,
RC ECO:0000313|Proteomes:UP000003477};
RX PubMed=22232617;
RA Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.;
RT "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes are
RT Distinguished by Strain-Specific Features.";
RL Front. Microbiol. 2:261-261(2011).
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}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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:EHJ12612.1}.
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DR EMBL; AESD01000397; EHJ12612.1; -; Genomic_DNA.
DR RefSeq; WP_007310860.1; NZ_AESD01000397.1.
DR AlphaFoldDB; G5J5B4; -.
DR PATRIC; fig|423471.3.peg.2516; -.
DR Proteomes; UP000003477; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 113..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 404..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 721..740
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 746..770
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 18..84
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 783 AA; 83757 MW; 335A7C82753086E9 CRC64;
MVQLSLKPES TTPQPLVETV TLDVQGMKCA GCVSAVEKQL TQQSGVVSAC VNLITEVAVI
NYEPQTVQAE TLAEKLTKIG FTSDIRTSQT LTPQQIHFNQ SQRREAEARQ QKINLITAAI
LLIFSALGHL EHFGGPTLPI ISSLGFHWGL ATMALLIPGR EVIIDGWRAL SHGMANMNTL
VGLGTLSAYI TSCVAFLFPI LGWECFFDEP VMLLGFILLG RTLEKQARNR ASSALEALIA
LQPSLARLVG DPFSEDSSSI EIPVEQVRVG EYVKILPGEK IPVDGEIITG KTAIDESLVT
GESLPIAKNP GDRAIAGTLN HSGVITLKTT EVGEDTTLAQ IIASVETAQT RKAPIQQLAD
TVAGYFAYGV MVLASLTFLF WYIFGTHWYP QVLNLDSLGM SSSPLLLSLK LAIAVLVIAC
PCALGLATPT AILVGTSMGS ERGLLIKGGD VLEKVHQLEG VIFDKTGTLT VGHPTVTDCI
SWGDIKPESL LQLAATVESG TNHPLGLAIL EKAQQQELPL LSARDFYTEA GSGVQAQVEG
KMVWLGNQRW LEDQGLSLDK NHDKLIGSLN RAGKTVVYLG IEGSIQGVLA LKDNLRTDAQ
KTVSELQKRG LEVILLTGDH PEVAQAIASQ VGITQVLAEI PPSGKAAVVE ELQKSKKVAM
VGDGINDAPA LAQADLGISL QGATEVAMET ADIVLMSNQL WDVITAMDLS LGTFRKIRQN
LMWALGYNTF AIPMAAGVLL PSLGLMLSPA MAAGFMAFSS VTVVTNSLLL RYRKFGLIKS
TLI
//
