ID H1KN51_METEX Unreviewed; 684 AA.
AC H1KN51;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MetexDRAFT_4064 {ECO:0000313|EMBL:EHP91043.1};
OS Methylorubrum extorquens DSM 13060.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP91043.1, ECO:0000313|Proteomes:UP000004382};
RN [1] {ECO:0000313|EMBL:EHP91043.1, ECO:0000313|Proteomes:UP000004382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP91043.1,
RC ECO:0000313|Proteomes:UP000004382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., Pirttila A.,
RA Frank C., Woyke T.J.;
RT "The draft genome of Methylobacterium extorquens DSM 13060.";
RL Submitted (SEP-2011) 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:EHP91043.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGJK01000135; EHP91043.1; -; Genomic_DNA.
DR RefSeq; WP_003602843.1; NZ_AGJK01000135.1.
DR AlphaFoldDB; H1KN51; -.
DR PATRIC; fig|882800.3.peg.4004; -.
DR Proteomes; UP000004382; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000700; PAS-assoc_C.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHP91043.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 246..298
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 318..539
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 560..673
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 611
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 684 AA; 74160 MW; FD1562AB72B995F3 CRC64;
MTALRSAPPF PQGFLNDVVA VESIAAVPTI LDVVCRTTGM GFAAVARVTE DRWVACAVKD
DIAFGLKPGG ELDLETTICH EIRQSGVPVI IDHVADDPTF CEHHTPAKYG FQSYISMPIV
LPDGTFFGTL CAIDPKPAKL NTPAVVGMFK MFADLIGFHL DANQSLASRT AERDLYENIV
QSHAEPICVF DKAYRLIAFN KAHNDEFFRV NGFYTKIGDV FPDLFIPEQA AAMRANMARA
LAGEAYTVEA VFGRAEFGQP CWEITYTPLR DAAGTIFGAF HQAHDISARL RAEAELRDAQ
DVLRQSQKLE VIGQLTGGVA HDFNNLLTVI KSSTDLLKRP DLAEDRRSRY IEAISNTVDR
AAKLTGQLLA FARRQTLKPK VFAACDSVRA LSDMLGTLTG SRITVVTELP ENACFVNADP
SQFDTALVNM AVNARDAMEG EGQLTIRVEP VEQMPSVRAH PAVQGPFVAV SISDTGSGIA
KDVVERIFEP FFTTKAVGQG TGLGLSQVFG FAKQSHGEVV VESEVGRGTT FTLYLPRVLG
EIQAPEPSEP TPVPSGRGTS VLVVEDNVEV GTFATQTLAE LGFGTVWAAN AAEALAELAK
DADRFDVVFT DVMMPGMNGV DLAREIQRLH PDLPVVLTSG YSHVLARTGT NGFELLQKPY
SVEQLSRTLQ AVAKPARRKR IGDV
//
