ID H1KUG7_METEX Unreviewed; 559 AA.
AC H1KUG7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=MetexDRAFT_6280 {ECO:0000313|EMBL:EHP82573.1};
OS Methylorubrum extorquens DSM 13060.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP82573.1, ECO:0000313|Proteomes:UP000004382};
RN [1] {ECO:0000313|EMBL:EHP82573.1, ECO:0000313|Proteomes:UP000004382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP82573.1,
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:EHP82573.1}.
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DR EMBL; AGJK01000393; EHP82573.1; -; Genomic_DNA.
DR AlphaFoldDB; H1KUG7; -.
DR PATRIC; fig|882800.3.peg.6027; -.
DR Proteomes; UP000004382; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 1.
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; 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: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; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EHP82573.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EHP82573.1}.
FT DOMAIN 1..56
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 61..131
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 193..418
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 441..556
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 491
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHP82573.1"
SQ SEQUENCE 559 AA; 61614 MW; 0343A545FB8A7EE7 CRC64;
GRDVRAERAW PRRDGSPRIA DIRYLPRPMP DGSTDGAYLF VTDISDAKRI EAMLEREVGE
RTRERDRLWQ TTNDLMGTAG LDGHLRSVNP AWGRLLGWSE QELLERPFLD FIDPEDHAGT
GAVLARLAGS DQITDFVDRI LSKDGRRRTV MWTAVPESGC FHIVGRDITD QRLAEEQLRQ
AQKMEAVGQL TGGIAHDFNN LLTGIIGSLD LMQTRIAQGR IDTLERYAGA ALTSAHRAAS
LTHRLLAFAR RQPLEQKPVD VNVLLAGMEE MLRRALPEQV HLDIVATEGV WPTLCDPHQL
ENAVLNLAIN ARDAMPEGGR LVVETSNAHL GPADLRLHSG AREGAYVCIR VTDTGHGMPP
EVAARAFEPF FTTKPLGMGT GLGLSMIYGF ARQSEGHARI LSEPGRGTTV TICLPRYRGA
LSSERASALP PEPARSERNE TVLVVEDELV VRDLVVEVLR ELGYRAIEAP DGPSGLEIVR
SSARIDLLVT DVGLPGLNGR QLADHARTLR PELRVLFMTG YAENATFGGG PLDPDMQMIT
KPFPVERLAA RIREMMELS
//
