ID Q64ZN3_BACFR Unreviewed; 647 AA.
AC Q64ZN3;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BF0294 {ECO:0000313|EMBL:BAD47043.1};
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD47043.1, ECO:0000313|Proteomes:UP000002197};
RN [1] {ECO:0000313|EMBL:BAD47043.1, ECO:0000313|Proteomes:UP000002197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46 {ECO:0000313|EMBL:BAD47043.1,
RC ECO:0000313|Proteomes:UP000002197};
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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};
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DR EMBL; AP006841; BAD47043.1; -; Genomic_DNA.
DR RefSeq; WP_011201926.1; NC_006347.1.
DR RefSeq; YP_097577.1; NC_006347.1.
DR AlphaFoldDB; Q64ZN3; -.
DR STRING; 295405.BF0294; -.
DR KEGG; bfr:BF0294; -.
DR PATRIC; fig|295405.11.peg.318; -.
DR HOGENOM; CLU_027708_0_0_10; -.
DR OrthoDB; 9797304at2; -.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0016020; C:membrane; 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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00512; HisKA; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAD47043.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:BAD47043.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..647
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004268169"
FT TRANSMEM 394..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 163..196
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 443..510
FT /note="Signal transduction histidine kinase
FT dimerisation/phosphoacceptor"
FT /evidence="ECO:0000259|SMART:SM00388"
SQ SEQUENCE 647 AA; 74921 MW; 6808727605F2986B CRC64;
MKRLVVLLFG LVGAALFMSA ANSGDRVLRD SIFHVYRSMP ADTIRTVFAK EAAMGHVKES
WALELLDSAL VFAREIKDVE GELELQYGIF RYYTFRMDGE NMEKTCATLR EACYRYKKYD
NYFLALHYVL QLKGSEGDTE YAILESRKMR EEAVRLHVDR GVFLSYITEG KSYVFARNTE
KAIEQYLKAL EIEGTTFGDK LMVHGYLASS YYLKDKYKEA LGELKAQRQL IDGVIKKKPS
MLGVYRSTLL TIELMYCKIY LGMVDADPLW IHLNEAAKFY DDDCFSATAV NYHFSWAGYY
YLRQDWERCF PEFERTLAAF KGTQPMYEIE IRRIMGDAYV DAGRYEEAAR AYKTAAVMCD
SVNKATLRMN EETVEANYRI RKALLDKELG EKRFLQVAVV GLSLFVVLLV WGVIRLIRIR
GELVKSQKEM AESYAVVVAT DKMKEVFLRN ITDEIRVPLD TVVELSDRLC RETNLKQEKQ
QEYSATIKKC ASKLIGLIFN VLDLARLESG MMKFVVEEYD VVQLCTDARL MVEMQTENRT
KVDFHTEPDM LLIDVDTNRF MKMLASVLKY PEESEGLFRV KFILSRPSED YLQIKVVNSP
IFMTAESEKE FDVLHTINRL YLETFQGSYQ LLEESGERMI IITYPVS
//
