ID I2GCC0_9BACT Unreviewed; 530 AA.
AC I2GCC0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN8_00473 {ECO:0000313|EMBL:CCH51544.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH51544.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH51544.1, ECO:0000313|Proteomes:UP000009309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309};
RX PubMed=22843583; DOI=10.1128/jb.00869-12;
RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T.";
RL J. Bacteriol. 194:4445-4445(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:CCH51544.1}.
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DR EMBL; CAIT01000004; CCH51544.1; -; Genomic_DNA.
DR RefSeq; WP_009280130.1; NZ_CAIT01000004.1.
DR AlphaFoldDB; I2GCC0; -.
DR STRING; 1185876.BN8_00473; -.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9766459at2; -.
DR Proteomes; UP000009309; Unassembled WGS sequence.
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; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCH51544.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009309};
KW Transferase {ECO:0000313|EMBL:CCH51544.1}.
FT DOMAIN 1..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 215..267
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 296..520
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 50
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 530 AA; 60348 MW; 22FD06FFBC2FB823 CRC64;
MILIVDDRRE NILPLKKILE LHRFVVDTAE SGEEALRKVL TTSYSVIILD VQMPDMDGFE
VANAIAGFSK ARFTSIIFLS AVNTEKKFIT KGYTSGGVDY LTKPVDADIL VLKVKTLHKL
YEQQQELRAA QDSLRKEVEV RKQAQEVLTE RMQELQGVLA SLPQVAFTVA SNGQLEYVNE
YWFRYAPSSS TFPAVYADDN VWDEWKRSLT DGGEFTREVR LKDLNTGDYR YHLLRIIPIR
QQGNLTRWIG TFTDIHPQKQ AAELLEREVE VRTNELRVKN AELERTNHEL QQFTWVVSHD
LKEPLRKIQL LNDTIKEKYL KDNPEATPYL DRTIRSSARM ATLINDLLSY TQLSAPEAFH
PTDLNSLLTD LLQDFEDVTA KKGAIVDVGP IPVLDVIPTR IRQVFQNLIS NALKFAKENV
PPVITIRAER IDTKDINGCP VPDGAYCRIV VQDNGIGFDE KFLDRIFVIF QRLHNRTNYE
GTGIGLAIAR KNIEKHHGII SARSRVNEGA SFILVLPVKQ AANESVSETR
//