ID A0A1H4DXP9_9BACT Unreviewed; 644 AA.
AC A0A1H4DXP9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444145_10687 {ECO:0000313|EMBL:SEA77564.1};
OS Alistipes timonensis JC136.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1033731 {ECO:0000313|EMBL:SEA77564.1, ECO:0000313|Proteomes:UP000183253};
RN [1] {ECO:0000313|EMBL:SEA77564.1, ECO:0000313|Proteomes:UP000183253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25383 {ECO:0000313|EMBL:SEA77564.1,
RC ECO:0000313|Proteomes:UP000183253};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNRI01000006; SEA77564.1; -; Genomic_DNA.
DR RefSeq; WP_010266674.1; NZ_FNRI01000006.1.
DR AlphaFoldDB; A0A1H4DXP9; -.
DR STRING; 1033731.SAMN05444145_10687; -.
DR GeneID; 78310510; -.
DR OrthoDB; 9796457at2; -.
DR Proteomes; UP000183253; 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; 1.25.40.10; Tetratricopeptide repeat 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 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; 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 SMART; SM00028; TPR; 4.
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 SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SEA77564.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000183253};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:SEA77564.1};
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..644
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010285477"
FT TRANSMEM 387..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 148..181
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 429..644
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 198..255
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 328..379
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 644 AA; 73428 MW; 89D209EAB296C6FA CRC64;
MKNALLLLAI LIASALPAAA QSAADGLDTT LVAYYRWCNR HKQDPEMLLK ADTMFRLAGE
RQNPRMQSVA LCLKTDYYYY TGNLDSLKVW VARTQQFTRE HDQLTHYYFV WTRLITYYSK
YSKYTLAQYE LERFRDQAIR DDYKPAIAEA YKQLGHIYRT KSLYDTAIES YAKSIGMVER
NNLKEVDASY LYLQLAELYT LQQKYDKAEE ALRMSEKRIL LPEHIWRTRI SRANLAAMQG
DFESAEEQVR EIREKSGGYV SENKIEEIEL TIYKGTRNFQ KALEIVNKQL ANYEMTKDSL
GSSHYFYIPM LASRASLLYE TGSYKAAAED LSRQAALARQ KYESDNQEML NEFATLFDVE
RHDREKVEAR QQAQAERLRR ARLFETGLGV ILLLATAFIV ILTRLNRGLA RAKRAAEESS
RMKGVFIRNI THEINTPLNA IVGFAELAST TPDDEPERSS YIDIIRENSG YLQKLIDDVL
YIADIESSEA PPSRAAVEVD TCCRRCIDEL SKHAPLATEI RFASDGEGRS PRIRTSCLLL
GKALTELLRN AVRFTDPKQG VGLSYSLSED GRSITFAVED AGPGVPEGER EHIFERFVKL
DSFNQGLGLG LAVCRLIART LGGDVRLDPD FTRGARFLLT IPTE
//
