ID G7LMS8_9GAMM Unreviewed; 581 AA.
AC G7LMS8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BrE312_2315 {ECO:0000313|EMBL:EHD21696.1};
OS Brenneria sp. EniD312.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD21696.1};
RN [1] {ECO:0000313|EMBL:EHD21696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD21696.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA Glasner J., Perna N., Woyke T.;
RT "Complete sequence of Brenneria sp. EniD312.";
RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; CM001230; EHD21696.1; -; Genomic_DNA.
DR RefSeq; WP_009112998.1; NZ_CM001230.1.
DR AlphaFoldDB; G7LMS8; -.
DR STRING; 598467.BrE312_2315; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_6; -.
DR Proteomes; UP000002759; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 1.10.1760.20; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:EHD21696.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EHD21696.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 452..554
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 581 AA; 64242 MW; B46EE920CB3DCB1D CRC64;
MSEIFEMLLA VFDRAALMLI CLFFLTRTRQ FRQLLQKDRH SPGERITVTA IFSLFALFGT
YSGINVEGSL VNVRVIAVVS GGILFGPWVG IATGTIAGIH RYLIDIDGIS SVPCLITSVI
AGVTAGYINK KVKKERQWSM GILGGMLCES LTMLLVVVWA TPTALGVEIV SKIAAPMILG
AVCIGLIVLL VQSVANEKEA IAARQAKLAL DIAHKTLPYF RNINSDSLTA ICNIIRSEIN
ADAVALTDTQ HILAYVGVGE EKYNIGQDII SPMTQLAIND GKIIIKNNDE QHLTPQIHSM
IVIPLWEHGQ VTGTLKIYYC HAHKITYSLR VMAVGLSQII STQIEVSRME QLRDMANKAE
LRALQSKINP HFLFNALNAI SSSIRINPDT ARQLVINLSR YLRYNLELND DEPIDIKKEL
YQIRDYIAIE QARFGAKLTV IYDIDDDLSY KIPSLLIQPL VENAIVHGIQ PCRGKGTVVV
SVKDRGDHLL VAVKDTGHGI SLETMERVAR NELPGNKIGL LNVHHRVRLL YGEGLHIRRL
EPGTEISFYI PRPDKQQPII PQTPGARATM NASVIQSGES Q
//
