ID A0A077FAI3_9PSED Unreviewed; 1096 AA.
AC A0A077FAI3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PSAKL28_23340 {ECO:0000313|EMBL:AIL61545.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL61545.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL61545.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL61545.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-2014) 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; CP009048; AIL61545.1; -; Genomic_DNA.
DR RefSeq; WP_038610441.1; NZ_CP009048.1.
DR AlphaFoldDB; A0A077FAI3; -.
DR KEGG; palk:PSAKL28_23340; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_6; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000028931; Chromosome.
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; cd13705; PBP2_BvgS_D1; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AIL61545.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AIL61545.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1096
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001718189"
FT DOMAIN 607..826
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 850..969
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 999..1093
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 899
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1038
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1096 AA; 120131 MW; 63D20BAFF53DE7B2 CRC64;
MNRLTALLLG CLLSLQTLLA FAIDVGEPRQ LLARSISSTT LALSAEDRNW LKHKHHLLLG
TTNPDYPPFD INVSNSDYEG LTADYAGLVS ELLGIPIEVR RFADRAQAIA ALHAGKIDLL
GSSNAFEAAD AQLVLSRAYT DDQSVIAIGS GKSLGLNDKL AGLRLAMVDH YLPTPVVTAL
YPQAKLQLYS SNLAGLSAVS LGKADAFLGD AVSSDYLISR VYLGSVQIDH FIKNLRGTFA
FAVSRNNSTV LRLLNQALDH IGDNDRLNIL RRWTSGSTRV LLNRSTLSLS AAERSWIEQH
PRVRVAINKY FAPMSFYDDR HQFRGITADV LDQISLRTGL KFDIQVVDTV AQMIQQVEHG
NVDIAGVLPP TPGREASLRF TRPYLITPRV LVTRADNSDL HSPEQLKGLR LALIRDFFPL
EAELRLRFPQ TTLVEVDDPL SLMESVAQGK ADVALSSQIN AAYFVSRMFK DRLQIASIYG
DQPGIASFAV ARNAALLHSI LDKALLSIPP DEMTELTGRW RTNALISDSL WYNYRGLILQ
ILLGAGVLIA AVIVWNRYLR KLIQQRSAAE QALQTELGFS KRLLEELRLA KEQAEDASRA
KSTFLATMSH EIRTPMNAVI GLLELAVQDA EQGRADRASL QVAFESANGM LELIGDILDI
ARIESGHMSL APQPTDLNAL VSATVRVFEG NARLKGLRLE SDLQSTQHLV LVDSLRLKQI
LSNLVSNAIK FTDQGSVKVS LRLHQREDGQ LQVVLEVIDS GIGISGEDQQ RLFQHFAQVG
AQTARQGTGL GLVISRSLCE LMGGTLNLHS ALHQGTRVQV TLNLALVLAE SAAHTDSKPQ
TSSASMPTQS ILVVDDYPAN LMLLERQLTV LGHRVIQAND AQQALALWQE SDFDTVITDC
HMPDMDGHQL ARQIRALEQR LQLPACLILG LTANAQAEER ERCLASGMNG CLFKPIGLAE
LRRHLQAGTS QVPLPETTDN DGNASGFDID NLQYLTLGDP TLIRRLVGEL ARSNHEDLNA
LRALGPQPSR SSLRALAHRI KGGAKMLKAR ALVRNCEALE QASLGDATDE QLKVLLDTLE
HSLLTLEKQL AQTLVL
//
