ID Q4ZNN3_PSEU2 Unreviewed; 434 AA.
AC Q4ZNN3;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Psyr_4209 {ECO:0000313|EMBL:AAY39239.1};
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY39239.1, ECO:0000313|Proteomes:UP000000426};
RN [1] {ECO:0000313|EMBL:AAY39239.1, ECO:0000313|Proteomes:UP000000426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a {ECO:0000313|EMBL:AAY39239.1,
RC ECO:0000313|Proteomes:UP000000426};
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY39239.1; -; Genomic_DNA.
DR RefSeq; WP_011268891.1; NC_007005.1.
DR RefSeq; YP_237277.1; NC_007005.1.
DR AlphaFoldDB; Q4ZNN3; -.
DR STRING; 205918.Psyr_4209; -.
DR KEGG; psb:Psyr_4209; -.
DR PATRIC; fig|205918.7.peg.4336; -.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR HOGENOM; CLU_000445_107_26_6; -.
DR OrthoDB; 9807021at2; -.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF08447; PAS_3; 2.
DR SMART; SM00086; PAC; 2.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}.
FT DOMAIN 166..218
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 363..434
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 49..76
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 434 AA; 49192 MW; 601EEE01E14A6CD7 CRC64;
MLHLFSPRRD KKALQQLISS LKGGTEPAVG GCAEKSAVLE CWSSLSTQRR LDEQRIAALE
QELETARHLL GEASASAAAY ETRFDLVNRA SSEGLWDMEV VAGDPVNPNN RFWWSQQFRT
LLGFNDERDF PNVLASWADR LHPQDKQASL DAFAKHLNDR SGNTPYRIKN RLAMKDGTYR
WFYAQGETLR DARGTPLRVA GSLRDIHDEL ERDLEHDVII TRFELAREML SDGLWDMEVI
AGDPVNARNP FWWSPQFRRL LGFETVEEFP DVLDSWASRL HPEDKERSLT AFGAHLNDRT
GKTPFDIEYR LKMKTGEYRW FRARGQTRRN PEGVPLRVVG ALVDVHLKHE QDALRDTEAQ
HQKNLEENIA QLTQIVGTIQ SIASQTNLLA LNAAIEAARA GEAGRGFAVV ADEVRKLATR
TTEATEQAAS MMSR
//
