ID I2GDH5_9BACT Unreviewed; 473 AA.
AC I2GDH5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN8_00908 {ECO:0000313|EMBL:CCH51949.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH51949.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH51949.1, 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:CCH51949.1}.
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DR EMBL; CAIT01000004; CCH51949.1; -; Genomic_DNA.
DR RefSeq; WP_009280535.1; NZ_CAIT01000004.1.
DR AlphaFoldDB; I2GDH5; -.
DR STRING; 1185876.BN8_00908; -.
DR eggNOG; COG5000; Bacteria.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000009309; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCH51949.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009309};
KW Transferase {ECO:0000313|EMBL:CCH51949.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 237..473
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 473 AA; 52240 MW; F84A2EB6B18A9D1F CRC64;
MGHFSVGLAW RLLLIVLLSG LMVYVYLQQA SGLLLLPLLI LHIVISVSLY RYVTGLNRKL
TRFLESVRYS DFTVAFRTDN ELGPSFRDLN SQFNEVLDAF RVARAEKEAN LHYLNTIVQH
VSVGLLTFDA AGQVELVNQA ALRLLGIYRL RHLNDLKNVH PELVELLQSP DRGPSVNVAA
PIVYQTGSRL KGSDRELSIR CASVRLRGRL VTVASLQNIR TELQQRELEA WQNLTKVLRH
EIMNSITPIV SLAGTMRDIV ETDLLPLPAG PNSADHNLNG NGSTFRPPDA AYADAVGDLR
DALMTIEQRG EGIMRFVDAY RHFTSIPQPV FDEVAVEKLL RHVAQLVQAD KPDFPITISV
ATPNLSIRAD GGQIEMVLIN LLRNAVESLG SKPDPLIQIS AAQDGTRVIV QVADNGPGIE
PEAMEQIFIP FYTTKKTGSG IGLSLSRQIM QLHDGQLTVE STVGKGSTFS LVF
//
