ID B1ZF38_METPB Unreviewed; 742 AA.
AC B1ZF38;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mpop_0092 {ECO:0000313|EMBL:ACB78285.1};
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB78285.1, ECO:0000313|Proteomes:UP000007136};
RN [1] {ECO:0000313|EMBL:ACB78285.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJ001 {ECO:0000313|EMBL:ACB78285.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-2008) 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; CP001029; ACB78285.1; -; Genomic_DNA.
DR AlphaFoldDB; B1ZF38; -.
DR STRING; 441620.Mpop_0092; -.
DR KEGG; mpo:Mpop_0092; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000007136; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; 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; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACB78285.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACB78285.1}.
FT DOMAIN 360..581
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 603..716
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 654
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 742 AA; 80599 MW; 9A1764DF2F953835 CRC64;
MRTSGCDPRS PGTGRRSRIA VGRGTPISGG VASVTDPIPF LPDGGLTGAE MRARDWEATS
LGPPGDWPPA LRNALTLMLE CPTAMFLAWG PDLLCFYNDA YRPILGYRLP TALGRPFPEV
WASIWTEIEP LVSATLAGRQ QVLTDLMLDL SREGKPEKSW WSFTYSPVRD DAGAINGMLC
VTKETTGHIS GQARLREMNE TLERRVDEAL AERKLWAQVF ETSDALVGAL DTGYRVLLLN
RALADEFETL FGVRPAVGDS LPELLADKPA HLAVAQAVWN RALAGEEFTR IEEFGDPTRK
RRSYEMRFTT LRDAEGRVVG AFQYATDVTQ RLREQEQLAR AEEALRQAQK MEAVGQLTGG
VAHDFNNLLT IIRSSVDFLR RPNLPEERRT RYMDAVSDTV ERAAKLTGQL LAFARRQTLQ
PEVFDVGERL GGVVSMLNSI TGARITIETA LPGRPCYVRA DPSQFETALV NLAVNARDAM
DGAGTLTLGV APVASMPPIR GHAGGNGAFV AMSVTDEGSG IAPDLLGRIF EPFFTTKEVG
KGTGLGLSQV IGFAKQSGGD VDVASEPGRG TTFTLYLPEV DPPKPAVEVE GDDDGPGEVR
ALCVLVVEDN LDVGSFCTQI LEDLGHSVVW AHDAEEALAE MEKVPFRFDA VFSDVVMPGM
GGVELARRLR ASHPDLPVIL TTGYSDVLAR DDAHGFDLVR KPYSAEQVAH AFRTVHVRRR
GREGTARSKA AAITGNSSSR VV
//
