ID G7CKT4_MYCT3 Unreviewed; 955 AA.
AC G7CKT4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=P-type HAD superfamily ATPase {ECO:0000313|EMBL:EHI11741.1};
GN ORFNames=KEK_12618 {ECO:0000313|EMBL:EHI11741.1};
OS Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI11741.1, ECO:0000313|Proteomes:UP000004915};
RN [1] {ECO:0000313|EMBL:EHI11741.1, ECO:0000313|Proteomes:UP000004915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC 316 {ECO:0000313|Proteomes:UP000004915};
RG Tuberculosis Structural Genomics Consortium;
RA Ioerger T.R.;
RL Submitted (NOV-2011) 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}.
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:EHI11741.1}.
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DR EMBL; AGVE01000046; EHI11741.1; -; Genomic_DNA.
DR RefSeq; WP_003926005.1; NZ_AGVE01000046.1.
DR AlphaFoldDB; G7CKT4; -.
DR PATRIC; fig|1078020.3.peg.2478; -.
DR eggNOG; COG0474; Bacteria.
DR Proteomes; UP000004915; Unassembled WGS sequence.
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; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000004915};
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 72..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..939
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..88
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 534..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 100998 MW; 4D0B63BC2E87F02F CRC64;
MAAPVVAAPD PTPDPALRDA ADIARELGVD PAVGLSTAEA ARRLRVDGPN ELRAKPPLPG
WRRFLAQFQD PLVYLLLVAV AISLLAWAAE GARGVPIDAV VISVVLMLNA VLGFVEEHRA
ENAVAALQSM TETRATVLRD GRLTTVPSHE LVRGDILVLN EGDAVGADAR VLSATALRVQ
EAALTGESEA VTKNAATLPR RVPLGDRRNM VFKGTAVVQG VGRAVVTGVG MRTEAGAIAE
LLEATEEEPS PLQKEITWVS KLLGVTVIAI AVAVMVLTAA VNDVDTVDEF VTVLLLGVAL
AVAAVPEGLP AILSVVLAIG VQRMTRRNAV VKKLHSVETL GSASVIATDK TGTLTKNEMT
IQRIRTASGE VELTGVGYRP DGTALLDGKA LTDPRLAREV SLVIAGGSIA NNAQLHRRDD
TWEIQGDPTE AAFLVAAHKL ADATELARAF RRRAEIPFTS ERKMMSVLGR AEDEPPTLVT
KGAPDVLLRR CAALQLGDDI VPLDDERRAR ALADVDELSA QGFRTLAVAY RRIGEPDLPD
DPDGPGIGDE ASGISDEVED DLVYVGVVGI IDPPRDEVPD AVAMARRAGI RVLMITGDHP
RTAVRIAEDL GLIDAGAEPG AGRAAITGAE LDDLSNRELL EVTARTSVYA RVAPQHKLRI
VDALQLQGHV VAMTGDGVND APALKSADIG VAMGITGTEV TKEAATMILG DDNFATIVAA
VRQGRIIFDN IKKFLRYLLS SNMGEVFTVF FGVLLAGYIG LTAGAGETIV VPLLATQILW
INLITDSTPA LAMGVDPEVD DVMARGPRRP GDRIIDGHMW AGIMSIGLVM AAVTLLTMDI
FLPGGLVEGS DSLDVARTAG FTTLVFAQLF NSFNSRSETS SAFRRPFSNP WLWAAVALGA
ALQVAVVHVP LLQVAFGTAP LDLAHWAVAI AMASVVLWFD EIRKVVLRAF GVDGA
//
