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Database: UniProt
Entry: H1KFH3_METEX
LinkDB: H1KFH3_METEX
Original site: H1KFH3_METEX 
ID   H1KFH3_METEX            Unreviewed;       338 AA.
AC   H1KFH3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MetexDRAFT_1385 {ECO:0000313|EMBL:EHP93704.1};
OS   Methylorubrum extorquens DSM 13060.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP93704.1, ECO:0000313|Proteomes:UP000004382};
RN   [1] {ECO:0000313|EMBL:EHP93704.1, ECO:0000313|Proteomes:UP000004382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP93704.1,
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:EHP93704.1}.
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DR   EMBL; AGJK01000024; EHP93704.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1KFH3; -.
DR   PATRIC; fig|882800.3.peg.1361; -.
DR   Proteomes; UP000004382; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50943; HTH_CROC1; 1.
DR   PROSITE; PS50113; PAC; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          84..136
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          271..325
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   338 AA;  37963 MW;  AF67758733730E60 CRC64;
     MPAAVSPIMP HEILRMVEGF GLTGTWSWTF ATDRHVWSPG LFRILGLEPT SARAEYGLLF
     ALVHPEDRDS ITSTSELLQT GHMIQQTFRI IRPDGTLRTV MSRGEVVMAP DGRPLQAMGV
     LIDVSDREML ARAQAADRRR KRALFEQTRA FTSVTAVYPY TDFSPEWLEL VGLPRQALLE
     EPTLPVLKEE RARWRDHGRE LYLTRQVVHT RPRLILASGE IVPYRMVMVP MRNASGADEG
     WVNYIAPLHL DGGVPGVMRE SLEQLVRGIH LRAGRALLDW SMQQLAEAAG LSFSTVRRLE
     DEDVSASRRA LQAAMRALRT HGIVFSFMDD GTIALGKV
//
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