ID H3SE08_9BACL Unreviewed; 587 AA.
AC H3SE08;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-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=PDENDC454_08785 {ECO:0000313|EMBL:EHQ62684.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ62684.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ62684.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ62684.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ62684.1}.
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DR EMBL; AHKH01000017; EHQ62684.1; -; Genomic_DNA.
DR RefSeq; WP_006676270.1; NZ_AHKH01000017.1.
DR AlphaFoldDB; H3SE08; -.
DR STRING; 1131935.PDENDC454_08785; -.
DR PATRIC; fig|1131935.3.peg.1798; -.
DR OrthoDB; 368131at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHQ62684.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..583
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 331..365
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 587 AA; 66680 MW; D9B2DF72F13E4052 CRC64;
MKSGRRLAWH YAWQWLLIGA MLLGCMFAAF LWVAERMSAL DMSRNLPTSQ LSRIVESVQV
DRQGRVVWPD EVFQRLTSSG GWLQVLNEDG KVVDSFNAPG DMPTQYAPGE AVAYVQGELP
SKYGIFIYIR SVGGRNITLL YGTYPPQLQL LDKWLASREK GIPAAESVRR LLVPHDAWVA
RLDAAGRTLE SWNKPAGVAE RLTLQEIALR SLQPEHYAHL LAYRYNPATG DTWVLQMPHQ
TEGAGVTAAG LRIASYQDIF FLAVGGVIAT MIIVFLFMAW WQSTRLARPQ LHVMRWTERI
ADGIYEEPAD HRGLPRSERR SGKLRRNYRI YEDVMQALRQ LASRLRSAEE ERRQHERQRE
EWLAGLSHDL KTPLASIVGY ARMLEAKQYD WSREEVAEFA GVMTEKAEWM DQLLQDLNLT
YRLQSGTLPL QRERLCLDAW LEETLDDILD LPQHPKALIH YQRPDIPVWF SFDPRYFRRI
IENICMNAFL HNPPGTALTI SFLARDGEDA LEFRDDGAGM DGETLSHLFT RYYRGLSTDR
AAEGSGLGMA ISRQLAEAHG CTLEASSEPG GGTVILLSLP GAEHRKI
//
