ID A0A345QUU0_9RHOB Unreviewed; 1495 AA.
AC A0A345QUU0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C1J03_23405 {ECO:0000313|EMBL:AXI49077.1};
OS Sulfitobacter sp. SK012.
OG Plasmid unnamed1 {ECO:0000313|EMBL:AXI49077.1}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389005 {ECO:0000313|EMBL:AXI49077.1, ECO:0000313|Proteomes:UP000253903};
RN [1] {ECO:0000313|EMBL:AXI49077.1, ECO:0000313|Proteomes:UP000253903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK012 {ECO:0000313|EMBL:AXI49077.1,
RC ECO:0000313|Proteomes:UP000253903};
RC PLASMID=unnamed1 {ECO:0000313|EMBL:AXI49077.1,
RC ECO:0000313|Proteomes:UP000253903};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter genomes from the North Sea.";
RL Submitted (JAN-2018) 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; CP025805; AXI49077.1; -; Genomic_DNA.
DR KEGG; sulz:C1J03_23405; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000253903; Plasmid unnamed1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd16919; HATPase_CckA-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Plasmid {ECO:0000313|EMBL:AXI49077.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253903}.
FT DOMAIN 36..219
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 238..477
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 862..933
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 990..1060
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1130..1352
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1373..1490
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 654..748
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 69
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1423
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1495 AA; 163709 MW; BE640E4BDC1E7DE6 CRC64;
MARKTSKLAV KGKPKPIRST VAKPKATANV EVAIPVVGLG ASAGGLQAYS AFLDAAPSDT
GAAFVLVHHV DPDHKSLMAD LLAKHTEMPV VLAVDQMPVQ ANHVYVIPPN SYLEIKKGVL
HLSEPTDRRG TRLPIDLFLR SLAKDLGQNA IAVILSGTGS DGSAAIREIK EQGGIVLVQD
PAEAQHDGMP RSAIATGATD HVVAVAEMPD IITSYVRHPF VKNDSAKKVL GENAKGSLEQ
IIAVLKAHSP INFDLYKDGT LLRRIERRMA LQHMENSGDY LALLKDSAEE AQNLCADLLI
SVTSFFRDPD AFDHLEKTVL EGLVKSHDAG HPVRIWVPGC ATGEEAYSLA MLVIEKISTL
RKDVKLQVFA SDVDERALTV ARNGVYPDSI AEDVSAVRLR RFFTKEDHSY RVTPELRDAV
VFANQNILAD APFSKLDLIS CRNLMIYLTP DAQERIIQMF HFALNDGGVL VLGMSETTGN
HDALFESLSK KYRVYKPVGH TRSRAFDFPI VQRPYANAGL VPTRSPFQAA GTKLAELSQS
LLVQHYAPAA VLINAQSEAL YFEGPTDKYL RVPSGETSRD LLAMARQGLR ARLSSAVRAA
RTQDAVVSER ATITRGDDRV GVTIQVHPVT LDEAKLFLVT FADEPMKVVV PAPNETNTEA
NRQLEQELET MRADLRTTIR DYELSTEELK AVNEEAMSMN EEFQSTNEEL ETSKEELQSL
NEELTTLNTQ LQQKIDDERR MSDDLNNLLS SSGIATLFLD TDFKIMRFTP ATRELFNLIS
KDIGRPFSDI TGKVKDPGLP KDAEAVLETL VSVECEVESD DGRWFVRRIL PYRTQSGKID
GVVVTFSEVS DLKALQHETA TARELAESII GTVREPMLVL DATFKILTAS RSFSRIFETA
AVDVIGKNLF SIQNRQWDVP QLRKLIESVL PDQTSVEAFE LTLNAGDLGR RQMVLNARRI
VGRPEHEESI LLAVEDVTDK NSAQQAILDR EARLSAILDA APEAILTIDE HGIVGTFSPG
AEEIFWFKAE EVLGQNVNML MPEPDRSKHD GYLEHYIKTG EKKIIGIGRE MDAGRKDGSR
VPIRLTVSEL ELDSARHFLG IIHDLTLDKK RQAELQRAQK MEAVGQLTGG LAHDFNNLLT
VVIGNLELLE MRTDDTKLHE LINEALEASN LGAALTSQLL SFSRSQSLAP EHVALNDLVN
TMLPILERTL DEQIAIETHL ADDLRATLAD PGQIESAILN LAINARDAMP DGGKLTVETR
NVALDADYAA AQVDVTPGDY VCLSVTDTGV GMSPETQSRV FEPFFTTKGP GAGSGLGLSM
VYGFAKQSGG HVVIYSEMGQ GTTVNLFLPI AAEAEAGQES AKLGNISASV GETILVVEDD
PKVLRLTVTR LEELGYQVIA ATNGPKAIDV LKRHEDIDLV LSDVVMPGGM TGFDVADQAL
ALRPDLKTLL ATGYAKGVEP RDAASIKTDH RILRKPYGMK ELARTLRELL DGSTL
//
