ID A0A2K9LRQ7_9GAMM Unreviewed; 889 AA.
AC A0A2K9LRQ7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=ATPase {ECO:0000313|EMBL:AUM14930.1};
GN ORFNames=Kalk_12420 {ECO:0000313|EMBL:AUM14930.1};
OS Ketobacter alkanivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM14930.1, ECO:0000313|Proteomes:UP000235116};
RN [1] {ECO:0000313|Proteomes:UP000235116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA Kim S.-J., Rhee S.-K.;
RT "Direct submision.";
RL Submitted (AUG-2017) 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; CP022684; AUM14930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9LRQ7; -.
DR KEGG; kak:Kalk_12420; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000235116; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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: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; 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:UP000235116};
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 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 783..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..64
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 889 AA; 96772 MW; 39F11FA9FB6A7E6C CRC64;
MNSLSSTQHG LTAEEAQQRL IQFGANQLPE APTRPALLRF AAQFNNVLIY VLLASGGISL
LMQHVIDATV IFGVVLINAI IGFVQEGKAE AALRAIHNMV RTECKVWRDH RVETLDSEML
VPGDVILLQS GDRVPADLRL FQVKDLRCDE SALTGESQPV TKSNGELAEA TPLAERSNMA
YTGTLVTYGT ALGLVVNTGV RTELGNIGTL VQQAEVPKTP LTRRLEQFAR QLTYIIIALS
GAMVLFGIFA RQYDLFAMFQ AAVGIAVAAV PEGLPAVVTI TLAVGVQKMA RLHALVRKLP
SVEVLGSVSV ICSDKTGTLT RNEMTATRLV LADCSLSVSG EGYGDVGNIL DAAQNSLRAD
DEQRLSLIAR TSLLCNTATV IRKDGQWQLS GDPTEGALVS LALKAGLTEE RAAQEWPRND
MLPFESERRY MATLHHNHQG EHEILIKGGP DRLLPFCSHQ LGCNGVEPLD ADHWNQSIEE
LASVGLRVMA LAYKPSPPVE ELTYDMVEQD LILVAVVGIT DPPRAEAIDA IRQCQQAGIR
VKMITGDNPH TAAAIARVLG LRTNRVLTGA DLDKTDLDTL PQQVQACDVF ARTSPEHKLR
IVEALQQQQH VVAMTGDGVN DAPALRAADI GIAMGRKGTD AAKDASDIVL TDDNFATIVA
AVRQGRTVYD NILKAILFIL PTSLAEASVI SVAILLGLML PITPAQILWI NMITAITLAL
ALSFEPSEPL SMNRPPRPIK QGLITGFVLR RLLFVGALGT LIVFGLFYLA LEQGASIEKA
RTVAVNTLVF FEIFYLFNCR TQTPLWQNPR PFGGIAVWIA VVTVVALQML FNYLPGFRDL
FQAKSLSLQE WLWVLAGSGS VLMLVELEKW LTLYRQKRTE TQTSRAGQN
//