ID C7GAU1_9FIRM Unreviewed; 437 AA.
AC C7GAU1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ROSINTL182_07021 {ECO:0000313|EMBL:EEV01109.1};
OS Roseburia intestinalis L1-82.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=536231 {ECO:0000313|EMBL:EEV01109.1, ECO:0000313|Proteomes:UP000004828};
RN [1] {ECO:0000313|EMBL:EEV01109.1, ECO:0000313|Proteomes:UP000004828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L1-82 {ECO:0000313|EMBL:EEV01109.1,
RC ECO:0000313|Proteomes:UP000004828};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2009) 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:EEV01109.1}.
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DR EMBL; ABYJ02000094; EEV01109.1; -; Genomic_DNA.
DR RefSeq; WP_006857123.1; NZ_LR027880.1.
DR AlphaFoldDB; C7GAU1; -.
DR GeneID; 61431372; -.
DR HOGENOM; CLU_000445_89_2_9; -.
DR Proteomes; UP000004828; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR031967; PhoR_single_Cache-like_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF2; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF16736; sCache_like; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EEV01109.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:EEV01109.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 9..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..437
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 437 AA; 48571 MW; E42E58B6E4A201E5 CRC64;
MKKRINTGFM LIAAIAIVVT AVCSMFLFYQ ILEEQIFDDL KASAHVVSVI SPNELSKDIT
YSLENDGLRI TCVDTDGTVL YDSMEDASSM ENHKERPEIA EAIKNGEGKS IRVSATSSKH
TFYYALRKED GSVVRVAKES GSIYHLVSTM SGLILAVGLM VFLMCVFYSY RLTRRLMAPI
GKMADNIILV DETEVYEEMR PFISMIKKQH MDILNHAQMR QEFTANVSHE LKTPLTAISG
YAELIASGMT GGEDTAHFAN EIHKSAERLQ ALINDIIKLS ELDDSDLKLE FETVDLHDLG
EQCIHSMQMQ ADKNEVTLHL EGASVPMSGN KTLLEELLFN LCSNAVRYNK KGGSVTIVTT
IENTRPVLIV KDTGIGIPKE QQERVFERFY RVDKSRSKST GGTGLGLAIV KHIVAQHDAQ
MTLTSEVGVG TEIKIVF
//
