ID J2PK15_9PSED Unreviewed; 845 AA.
AC J2PK15;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMI22_01061 {ECO:0000313|EMBL:EJM23739.1};
OS Pseudomonas sp. GM21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144325 {ECO:0000313|EMBL:EJM23739.1, ECO:0000313|Proteomes:UP000007292};
RN [1] {ECO:0000313|EMBL:EJM23739.1, ECO:0000313|Proteomes:UP000007292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM21 {ECO:0000313|EMBL:EJM23739.1,
RC ECO:0000313|Proteomes:UP000007292};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM23739.1}.
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DR EMBL; AKJS01000022; EJM23739.1; -; Genomic_DNA.
DR RefSeq; WP_007943542.1; NZ_AKJS01000022.1.
DR AlphaFoldDB; J2PK15; -.
DR PATRIC; fig|1144325.3.peg.1026; -.
DR eggNOG; COG4191; Bacteria.
DR Proteomes; UP000007292; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 3.
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; IPR013656; PAS_4.
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; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
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; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
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 107..160
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 249..301
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 302..372
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 372..426
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 478..703
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 726..841
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 417..469
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 776
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 845 AA; 93881 MW; C5E13F78383CFE37 CRC64;
MNAAPTGSDA LALIARLDWT STPLGAAGTW PQSLRTAVDI VIHSPMPMLL LWGPQLTQIY
NDGFAFLAGS KHPHAFGQPT HQIWPELQDF TDPIYSAVLQ GQVRTYSEQR FTLQRDGEAS
DFWLDLTYSP IRDENAEVAG ILVTAIETNE RRRIALELEQ RSAASLKAQR DTEQRLQLAL
AATDAVGTWD WDIGEDRFLA DAHFAQLHGV DPGMAGHLPI SEYLHGVHPE DRALIARSIK
HCITHGTEYA EEYRLLQPDG QVRWVFARGR CYKDHHGRPM RFLGAALDLT ERKHTEQALR
QSQTELQLII NAMPVLISYV DSEERFRLNN AAYLDWYGLT PQELYGKTIR EVLGEQAYAL
RAEYIADALK GKPCCFSIST PHRDGSLRQA LMNYLPRHGA DGAVNGFYIF VIDETERKQT
EEALRNLNET LEERVAARTQ QLAQANQRLQ NEMFERERAE DALRHAQKME AVGQLTGGIA
HDFNNMLTGI IGSLDLMQRY IAEGRTDEIG RFTDAAVSSA NRAAALTHRL LAFSRRQSLD
RKPLNTNELV RSLEDLLSRT KGDHIELSLQ LADEVWPIST DVSQLENALL NLVINARDAM
PDGGKLLIET ANVYLDGNDL STLEPVRAGD YVMIAVSDNG TGMTPSVLAK AFDPFFTTKP
IGQGTGLGLS MIYGFAQQSG GHASLFSLPG KGTSVRLYLP RLHDMEPQDV LMPVKSEAPA
AIAGETVVLV EDDPAVRMLV LDLLNKLGYH AHEAEDAKTA LPLLESDLRV DLLVTDVGLP
GMNGRQLAEI ARQHRPDLKV LFMTGYAETA AERQGFLEEG MDMVAKPFSI DLLANKIRTM
IGQPE
//
