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Database: UniProt
Entry: A0A0A1MKY6_9BACI
LinkDB: A0A0A1MKY6_9BACI
Original site: A0A0A1MKY6_9BACI 
ID   A0A0A1MKY6_9BACI        Unreviewed;       586 AA.
AC   A0A0A1MKY6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=ypdA_1 {ECO:0000313|EMBL:CEI80534.1};
GN   ORFNames=BN997_00338 {ECO:0000313|EMBL:CEI80534.1};
OS   Oceanobacillus oncorhynchi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI80534.1, ECO:0000313|Proteomes:UP000040453};
RN   [1] {ECO:0000313|EMBL:CEI80534.1, ECO:0000313|Proteomes:UP000040453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oc5 {ECO:0000313|EMBL:CEI80534.1,
RC   ECO:0000313|Proteomes:UP000040453};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CDGG01000001; CEI80534.1; -; Genomic_DNA.
DR   RefSeq; WP_042529064.1; NZ_CDGG01000001.1.
DR   AlphaFoldDB; A0A0A1MKY6; -.
DR   STRING; 545501.BN997_00338; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000040453; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:CEI80534.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000040453};
KW   Transferase {ECO:0000313|EMBL:CEI80534.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          471..579
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   586 AA;  64765 MW;  F2074A5BA5677F4F CRC64;
     MMDLTMVLFE RLGLLLVIAF VLTRIPGFRS LLYREFSFKM AGIHACVFGI FGIAGTLTGV
     VIGSDFTVTH AFVWEVEADQ MVVSSSLVAI VMAGLLGGPA VGLGAGIIAG THLFFLGGIG
     FMANSLVNPL TGLLAGFTAR FFSQERVISP IKALFIGIFP PILLMHLLLI FDSLDRTMVE
     LINTIGLPVV LSNSIAIAIF TAMIAIVLRE QENEAAFATR QALTIAEEAL PFLKEESFQK
     KAEGIADLFY ARLKLAAVTV TNDKEVMAHK GLGGDHHRIG NPLITQISHQ ALESKEILVA
     YSQAEIQCTH KKCPLEAVII IPIWEAQQTI GLIKLYFRKP QHIRPVELML AEGLGQLIAN
     QLKTIKAERL ELHTRDAELS NLQAQINPHF LFNTLHMIAA LFRKEPEKAR HITVQLAHFM
     RFNLKLVSTQ LVPLEKETEH VKAYIEIIQT RFTGRMQIHF IQPEEMSHLL IPPSSIQPLV
     ENSVRHGLEH VSEGGRVDVK MEQVGKWIKI SVQDNGQGFP DSILLQAGEK VLTGKPHGGT
     GLYNVNQRLI NLLGEESRLH VRNLSGGGSE VHFTIPAVNT RKEDDL
//
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