ID A0A0C5WGL4_9GAMM Unreviewed; 787 AA.
AC A0A0C5WGL4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=H744_1c1219 {ECO:0000313|EMBL:AJR06243.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06243.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR06243.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR06243.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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};
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DR EMBL; CP005973; AJR06243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5WGL4; -.
DR STRING; 658445.H744_1c1219; -.
DR KEGG; pgb:H744_1c1219; -.
DR PATRIC; fig|658445.3.peg.1319; -.
DR HOGENOM; CLU_000445_104_15_6; -.
DR Proteomes; UP000032303; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR033414; Sensor_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF17149; CHASE5; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..228
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 250..471
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 488..609
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 664..782
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 542
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 713
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 787 AA; 88125 MW; 617148C1E12B505D CRC64;
MTRLLKKSRR ISLAKQLLFL IILLSSIFTL LFTSLSLFLE YKGELREIDN RFTQIQDSYL
SSLTSSLWVE DRELLQTQAE GVLSLPSISY VKVIDGDQVI IELGDFLNEG MLERQWLLSH
QAAKKDFRLG TLLVQSDLQP VYQNLYDTFL LLLFGHSLQI FFISVCILLI AYRLVVQPLT
KMSLAVTKFD DQNVPLPVQL SKRWCDDEIT TLASQYNQSA EHIRHHYLEL EAAKKAAEQA
NLKKSEFLAN MSHEIRTPMN GIIGLSGLMK DMEMPDNQKD YINMLHTSSM SLLDLINDIL
DFSKIEAGQF ELESIPLNLF ELNKEVESLF LLKAAEKGLN FSCSVEKTIS PMLMGDGAKL
RQILNNLVSN AIKFTDKGEV SLVMAHVESS DDSCKVQFRV SDTGIGVAED KQAAIFEKFQ
QADGSTTRKY GGTGLGLAIC REMVKMMGAE ITVDSTPGKG STFSFVIELP REKTSIPQEE
RFIFDGLNIL LVDDSMLNMR ITTVQLEGFG AKAVSCLDPN MAITMAEQAA SQGQAFDIVI
IDKFMPILNG FELAELFRQH FGESCPKLLM ITAVPEINDE EKAASCGIKS FLTRPYKDAH
LKWAILKLVA LPPESPHPDR ILEGEVHNID LSADTSELAH HEQAQADISV RKNALQQPND
MAVKVLVVED TLINQKVARM MLEKVGAVVD IVENGELAVS IYQEKRFDVI FMDCQMPVMD
GFEATRQIRG IEQQTGHFTP IIALTANVVK EEREKCFAAG MNDFVSKPVS LQVLKQKLEQ
HASLSVS
//
