ID A0A1H2MVC0_9PSED Unreviewed; 722 AA.
AC A0A1H2MVC0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=SAMN05216202_2464 {ECO:0000313|EMBL:SDU97187.1};
OS Pseudomonas mucidolens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46679 {ECO:0000313|EMBL:SDU97187.1, ECO:0000313|Proteomes:UP000198600};
RN [1] {ECO:0000313|Proteomes:UP000198600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 2223 {ECO:0000313|Proteomes:UP000198600};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; LT629802; SDU97187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2MVC0; -.
DR STRING; 46679.SAMN05216202_2464; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000198600; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF07536; HWE_HK; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 2.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 97..149
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 150..195
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 273..343
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 347..399
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 400..440
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 477..529
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
SQ SEQUENCE 722 AA; 79762 MW; C0E74358883CB6B6 CRC64;
MTNIQELPTE LSEFDRLVSM STDTLDAFPG AVYLCDQDGW LVSFNTEAAR LWGRAPVLGS
SGDRFCGSYQ LFLLDGTPLA AQDCPMASTL KTGVESRNAD VIIQRPDGSR FVALVNIRAL
RDKRGAIQGA INCFQDVSAH HAMAQELRLK SADLEDFFDN SAVGLHIVSG EGIIVRANKA
ELSLLGYAAD EYIGRPVTDF HADAHVIDDI LNKLGSGESL ESYPARLRAK NGSIKHVLIT
SNARIKEGTL FNTRCFTVDI SDVHAAEMAR RESDGRLSAT YEAATIGIAE ADSEGRLLRV
NDALCDMLGR RREQLLAMAF FEYTHSDSVE QDSGLYARQV AGELENYVLR KRAFKPGGEI
VYLDVHSSSV RDSSGNFRYG VRVIQDVTAA HRMQKQVRES ERHMRALLEA LPAAVYTTDA
EGRITFYNRA AVELAGRTPQ LGDMWCVTWR LLNVDESPLP HDQCPMAVAL KENRPIRGVE
AIAERPDGTR VPFIPYPTPL HDANGELVGA INMLVDITER KQAENRQKTL IDELNHRVKN
TLVTVQSIAS QTARNADSAE EGYQRFETRL LALSRAHNLL TKRHWGKSPL DSLVREVVAP
VFGHDPSRLL IEGPSIDVNS RVALNLTMTL NELAINALKH GAMRVETGSL SILWSTQPHA
DGIILSLEWR EHGGPKTSEP KTRGLGLRLM ARCIERDLDG NFELSFAPEG VVCRLSFVIG
AQ
//
