ID F3YY42_DESAF Unreviewed; 1051 AA.
AC F3YY42;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Desaf_3537 {ECO:0000313|EMBL:EGJ51818.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ51818.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ51818.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ51818.1,
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; EGJ51818.1; -; Genomic_DNA.
DR RefSeq; WP_014261432.1; NC_016629.1.
DR AlphaFoldDB; F3YY42; -.
DR STRING; 690850.Desaf_3537; -.
DR KEGG; daf:Desaf_3537; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_284372_0_0_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 5.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13426; PAS_9; 2.
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; 5.
DR SMART; SM00091; PAS; 4.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGJ51818.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transferase {ECO:0000313|EMBL:EGJ51818.1}.
FT DOMAIN 110..162
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 195..230
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 231..284
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 285..334
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 410..481
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 482..535
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 536..581
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 608..660
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 678..901
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 929..1046
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 978
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1051 AA; 116717 MW; 1FDE8DDE3A462766 CRC64;
MPGIEKSRQE LLAEAALLKE RLRELGRERD FLASLVESAS DEIWFCAPDE SFARPLNKAA
RDFLDLARAG LPPLQRAEAD SPLPIFKTQA ALLSPAESPL RRALAGETVH GDEAVLLPES
GEVRHREYRA SPIRDEQGAV SGAVAIARDV TKTRKAEAAL RESDESFQVA LTHTPVMVFA
ADMDQRFSWV FNPPFGLTAE EIIGKTLQEL IKPEDASEVQ ALVSELIESG RAIRQEVVIR
FRGRETCWDV TIEPRRDVRG VISGLIGVAY DLTERRWAEK AREQSDEKFR RIFHLSPAIL
AISTLQDGVY LDVNEAFSKL LGYSREEVTG KNAFELQLWA EPAQRNLLAA QLKERGSLRS
RLVRYRCKSG EIKTLVISAE LMEVEGQQCV LAAASDFTMQ QRRHDAIRKR EMEWRAIVEN
TSDIIARIDH ESRYTYINQA VTKVTGLLPR EIVGEAFHTR GFSGENLVKA KRALKTVFDS
GKPGLLELAA SGQGRPVTLQ VCLVPEFSRT GEVETVLAIS RDISELKQTE QELRSSREHY
RLLYESVPLG YQSLDARGCY LEVNQAWLEA MGYSREDVIG QRFGRFVTES AAYLAESFAA
FKQCGEISGA EFEMVRKDGS RFIAAFYGKI STDEQGRFRQ THCIMHDVTA RRRAEEEIRR
AQSAAEAASR AKSMFLAHMS HELRTPLNGI LGMVELAHMA CADEKQCKYL ELAKQSGHTL
LDIINDILDL AKIEAGKAEL KNEPFSLREV MESTIEPLAM LGRRKGLEVT WRMDPRIPDR
LAGDQGRLRQ VLANLVGNAL KFTERGSVSV DLGLSRGGFE TRPYCPAGMR LIFSIADTGI
GIPQDKLPHL FESFTQALTS AHVKFGGTGL GLCISKRLVE MMQGTIWAES VVGKGSTFSF
TAVFCVPQQP TLPEAAPACG PGVQGRRLRV LVAEDNQINQ VLIRELLGMQ GHTASIVGTG
LEALQALRQA EYDLVLMDIR MPDMNGLQAV QRIRAGEAGK TDIPVIALTA YALEGDRKRF
LAAGMDGYLA KPIRIEEFNT VLRDVAGRAS G
//
