ID C9L8L3_BLAHA Unreviewed; 566 AA.
AC C9L8L3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BLAHAN_05735 {ECO:0000313|EMBL:EEX21705.1};
OS Blautia hansenii DSM 20583.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=537007 {ECO:0000313|EMBL:EEX21705.1, ECO:0000313|Proteomes:UP000003755};
RN [1] {ECO:0000313|EMBL:EEX21705.1, ECO:0000313|Proteomes:UP000003755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20583 {ECO:0000313|EMBL:EEX21705.1,
RC ECO:0000313|Proteomes:UP000003755};
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 (SEP-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:EEX21705.1}.
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DR EMBL; ABYU02000017; EEX21705.1; -; Genomic_DNA.
DR RefSeq; WP_003021299.1; NZ_GG698589.1.
DR AlphaFoldDB; C9L8L3; -.
DR STRING; 537007.BLAHAN_05735; -.
DR KEGG; bhan:CGC63_08145; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_0_9; -.
DR Proteomes; UP000003755; 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; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEX21705.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 271..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..350
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 461..560
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 566 AA; 66094 MW; 0CB9D0CEE27E10F4 CRC64;
MKKWIQKYKD LKYRYKLTIM MILCSLIPVC VISAYTQMRT IQIMREKEES GLKQVLEQSV
DSIDNRVQIY TNLINYLTYS SDLREIMEKE YRSDYEAYLA YTEIADPLFT MPQLYHEEIR
SITLYAENIQ VEHGNTLAPL SVAQNQTWYS KINEKGTVQW LVKQGNKKEI LAVRKFYRQD
SIQAMLVLTL DYNRVLEPFA DLLTENRGGL ILDEQGNVVY SGYRMDAPYK PDKETSLNYL
KEHYVCIEKK IEDTKWNFCL YQPKEELEKS VWTLLLGNIP VLLLCLLLIL LLGYFFSRKM
VERLEQLTEN MNQINLGLRK VTVVSQSKDE IGVLVRTFTR MMDEINKLIS QVYEAKTKLQ
KTEMKALQAQ INPHFLYNSL SIINWKALEA DNEEISRITL ALSTYYRTSL NKGETMTIAA
NEIRNIDAYL QIQLIMHDNS FQVIKEIQED ALSYSVPKLI LQPLVENAIE HGLDVSEKEE
KWLKISVCKE KDALIMAVED NGMGMSEEQA KSIITYRSKG YGVRNVNDRI TLLYGEEYHL
RVKSRQGEGC RIEIAIPVNK EEKRYE
//
