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Database: UniProt
Entry: A5D4L5_PELTS
LinkDB: A5D4L5_PELTS
Original site: A5D4L5_PELTS 
ID   A5D4L5_PELTS            Unreviewed;       445 AA.
AC   A5D4L5;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=PTH_0654 {ECO:0000313|EMBL:BAF58835.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF58835.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF58835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D4L5; -.
DR   STRING; 370438.PTH_0654; -.
DR   KEGG; pth:PTH_0654; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_0_9; -.
DR   OMA; RVARNEM; -.
DR   Proteomes; UP000006556; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   Pfam; PF15714; SpoVT_C; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          326..427
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   445 AA;  49233 MW;  376F08B047DE1CFA CRC64;
     MRNLYDIAVG IAFRWAAVQL AAVAVVLLLV PVLWGGIALM VLASALSTYM VVDYIQKHKG
     VKVKLDDHPI DPTLQIANET LPFMRRGLNE ETAQKIAEII LKISDVSAVA ITDREKVLAY
     IGEGSDHHKA GGPIITYATK QALETGELII IKDKKGLNCP EKNCSLQAAV IAPLKCKGEV
     AGTVKLYQTS QGDLQPAVVK LTVAVAQLLG LQMELAELDR QAQLVTKAEL EALHAQINPH
     FLFNTLNTII TYSRTHPETA RRLLIRLAAF FRQALKRHGH FNTLREEIEY VNTYLILEKA
     RFREKLRIHR EIDPALLDYH VPVLTLQPII ENAIKHGIQP KMGTGTVQII ARLFNGEMLF
     IIKDDGVGIN RDKMPKIFLP WFGSGNGVGL SNVHERLKSL FGEDYGLRIV SEEGKGTSVY
     IRVPLNANTT ERGGQAGETQ SAYCG
//
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