ID L1QJN3_9CLOT Unreviewed; 608 AA.
AC L1QJN3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0216_00994 {ECO:0000313|EMBL:EKY28151.1};
OS Clostridium celatum DSM 1785.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY28151.1, ECO:0000313|Proteomes:UP000010420};
RN [1] {ECO:0000313|EMBL:EKY28151.1, ECO:0000313|Proteomes:UP000010420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY28151.1,
RC ECO:0000313|Proteomes:UP000010420};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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 -!- 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:EKY28151.1}.
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DR EMBL; AMEZ01000026; EKY28151.1; -; Genomic_DNA.
DR AlphaFoldDB; L1QJN3; -.
DR STRING; 545697.HMPREF0216_00994; -.
DR PATRIC; fig|545697.3.peg.979; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_1_9; -.
DR Proteomes; UP000010420; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; IPR033479; dCache_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; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKY28151.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010420};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 30..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..392
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 499..607
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 608 AA; 70599 MW; 0A580836FE96C1A8 CRC64;
MFTYCNYIFL GIYLLGDHMT LIKNSSIKKL TLSIFATLYL IFFIFTILNL YSYSKYESLK
TEKLIKNFNL SLSKQISEKI NSISDVSKYP LLIPEISNLH NILRSDNVLD INNYNYLKHL
CEMILIQNDS INGAYIYDLK GRGTFASRNT STDILINPSL EWWFLKSIQS DNSTSIFSNI
NIKSIVDVNT SSNENLIALT RQIIDISSNE ITGLLLITIP TDKILNLLNN DIAFNNQILS
LYDSDGQLIA ETNKNPLFND LYQNTQLITT NTEPQIEYMY KDTSYIVTYN YIQFYDWILI
NTIKKSDAFN LNTLYMMFFF INLIFFLIMS AILYLFLKNR IFNPIESLAK NMKSSNLEKN
LDTKIIYDKD DEIGFLVNSY NKMKNRINYL ININYKNALE HKELELQQLQ NQINPHFIYN
TLESIHMMAE INDDIETSTM AEYFGEIIRY SMNRRINTVT LKEELKIIDN YIYLQKIRFD
QLFTIENMVS DELLSCEIIK MIIQPLIENA IYHGLSECSG NGKIIIQGSK VNNNLLLTIS
DNGIGIPEEK LQDLNDYIND KNHNFNGIAL RNINKRLKLN YGENYGLEIF SIEGNGTSMV
LTLPFIIK
//
