ID F3YYP7_DESAF Unreviewed; 508 AA.
AC F3YYP7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Desaf_3594 {ECO:0000313|EMBL:EGJ51873.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ51873.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ51873.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ51873.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
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; CP003221; EGJ51873.1; -; Genomic_DNA.
DR AlphaFoldDB; F3YYP7; -.
DR STRING; 690850.Desaf_3594; -.
DR KEGG; daf:Desaf_3594; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3920; Bacteria.
DR HOGENOM; CLU_000445_114_57_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGJ51873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transferase {ECO:0000313|EMBL:EGJ51873.1}.
FT DOMAIN 123..177
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 178..222
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 249..301
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 312..506
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 508 AA; 57260 MW; 0E428452A19F7C29 CRC64;
MPLSAILSFL RRFPALRKAD ERDALKKLNT LHSRIRKTIA TMSEREQLLT ERNEEQKLLL
DNIDLQVWFL RAPDLYGAVN QAHAEFMGPD KAFLERHRLT DFLPPEEANR FACHNATVFR
FREPVSFSSF QQDARGRARI LSIRMTPRLS PGGAVEYAIC TAEDITKRIA AEQRLRRSEE
RFRGMFESIR DVYYRTELNG LITLISPSAE ALLGYAPGEM TGHLSTEFWA DPREFETFRE
LLLARSDIRD ATILLRHKNG QIIPTSMSCR LELGPDGEPA GTSGVLRDIS ERVSIEERLR
ASLKEKEVML TEIHHRVKNN LQVISSLLQL QSSQAGDPQL EALFAESQNR ILSMAYVHEE
LYKSGDLAHI NLKDYVQRLA RRLVQALAHT RPIGLELALQ DIQVTIDQAV PCGLILNELI
SNALEHAFEG RAQGRIIVSI SLDHGLARLM VSDDGKGVPA DFDPASSTSL GLQLVVRLAR
QLRGRVELDS QTKPGASFSV EFPLQAKP
//
