ID A0A2M9E1G1_9GAMM Unreviewed; 647 AA.
AC A0A2M9E1G1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CO641_13095 {ECO:0000313|EMBL:PJJ96782.1};
OS Xanthomonadaceae bacterium NML91-0213.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032582 {ECO:0000313|EMBL:PJJ96782.1, ECO:0000313|Proteomes:UP000229012};
RN [1] {ECO:0000313|EMBL:PJJ96782.1, ECO:0000313|Proteomes:UP000229012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML91-0213 {ECO:0000313|EMBL:PJJ96782.1,
RC ECO:0000313|Proteomes:UP000229012};
RA Bernier A.-M., Bernard K.;
RT "Zoonotically transmitted species of Xanthomonadaceae : Genome sequencing
RT and assembly.";
RL Submitted (SEP-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJJ96782.1}.
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DR EMBL; NWQL01000005; PJJ96782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9E1G1; -.
DR OrthoDB; 9768069at2; -.
DR Proteomes; UP000229012; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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 InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 22..92
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 95..147
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 278..495
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 516..632
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..285
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 565
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 647 AA; 71953 MW; F87C9051BCD38F1F CRC64;
MPITRSRRQV STAPGPGMPA NEPIEMRSLA DDAPAILWVT DACGHCSFLS RGWYEMTGQG
EDEALGFGWL DALHADDRPV VRARFARATR SRKAFTLDYR VRGRDGRYRW VLDAANPRHA
ADGSFAGFAG SVIDIDGRRR SEDNYRALFN SIEDGFCIFQ VLFDERQQAR DYRFIEVNPA
FSRHTGLVDA VGHTAREMLP DLEEHWFETY GRVALTGEPH RFEMESEAMD RWFQGYAFRI
GDPADRMVAL LFTDVSTRRR QEHALRDAER RKDEFLATLA HELRNPLAPI RTSLYVLKLN
EDPETTTRML DILMRQVDQL THLVDDLTEV SRITRGRIEL RAVDIPLAAV LRNAAESVQP
TLEQGRQSLE IDLPAEPLWL RADPVRLGQV FVNLLNNAAR YSREDTTIRV SARVEGGEAV
VSVRDEGMGI AREHLQSIFD LFTQVDRQHS ADTRGLGIGL ALVRSLVQMH GGSVTARSEG
QGRGAEFIVR LPLQRAGHAS QAPVEEAAAR PFAGLRVLVA DDNRDAAESM GEWLSAFGAE
TIVVHDGHAA LTMAQMHLPH VALLDLGMPE LSGLEVAQRL RTVPGAARMR LIAITGWGQA
RDRAGTEAAG FDHHMTKPPD IALLRSLLQD AHRELAVPAS ANGSAVD
//
