ID F3YYX3_DESAF Unreviewed; 1143 AA.
AC F3YYX3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Desaf_1279 {ECO:0000313|EMBL:EGJ49618.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49618.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49618.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49618.1,
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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003221; EGJ49618.1; -; Genomic_DNA.
DR RefSeq; WP_014259416.1; NC_016629.1.
DR AlphaFoldDB; F3YYX3; -.
DR STRING; 690850.Desaf_1279; -.
DR KEGG; daf:Desaf_1279; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_15_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGJ49618.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 69..139
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 280..330
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 331..401
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 404..456
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 640..861
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 886..1005
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1048..1141
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 935
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1087
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1143 AA; 125239 MW; 6E1D917C2F3047FE CRC64;
MTGQHVSCPA TLAALRRKAE LLLARLEAGL SGPDHLVLRE LLRELEAYEA GLQRQDLRLA
QIQGELEASR DLYSRLHDFA PIGFFSFDRS GTILQANLAG ADLLGVQREY LLGRSFTAFV
AEEDQSAFLA HGEAAFASSA TAATARCELR LSPRGGGVRH VQIASAVMPD RPDALGLSSR
DGRFCLSAVQ DITARVQADR ALKDSEEKYR GIFENAPLGI FRATRQQSYT SVNPAFARMH
GYESPAQLLA ETGDAACRYC ADPAERQRFL DRVDSQGLVA NQESCRLRRD GTKFWALTTL
KAAGTPQEPY YEGFVADISQ RKAAEEALRR SETRFRSLFE TAGSLIVLLD VNLRILEFNR
KAEQVTGYAR SDVLGQEFST LFAPEAREEL GARLLSVIGH RRERDLEQVV RGRDGRISVI
LWNMTRLEGS PESLNGVIAV GQDITAQKMA EKQLRLNQAR LEALLSLFQV EDRQARDMAE
YVLGQAVDLT GSEAGRILLA TGEEDLDIVT TGLPGRECPV TKQAHDLSAL SGVWSIAARS
KRPLVINDYA RRSRRRPLPE GHPPLRRLLI APVLDSGRVV AMAAVANKAA PYDQLDAKQL
MLLLEGLWAH VKRKQATLEI LQAKEQAEAA SRAKSEFLAN MSHEIRTPIS GILGMADVLL
TTRLEDRQAQ YIALLKDSAN ALLIIINDIL DLSKIEARKL KLEPELFNLD AALRAVVDPF
VLQTVKKGLG LEVHLDPGLP PKLHGDPIRL GQILTNLLSN ALKFTSRGGV TLRVVPVQVS
GVDCELRFEV QDTGLGIPSD KQDRLFRSFS QLDSSYAKQY CGTGLGLAIS KNFVEMMGGR
IWVESIEGQG SLFAFTAKFG LPDGGAQAAE NRREEALALD HMPTLNILLA EDNRINQEFL
VHMLGAAGHR SRVAANGREA LQALAEETFD LVLMDVQMPE MDGLETTRRI REHDGRLFDP
AIPIIAVTAY AMKGDQERFL AAGMDGYVSK PVDFGLLSRV MARVLFFHDP VVESASTEAL
DLPARNGLPA KAAKTLDVET ALGRLRGDRE LYAMLLETFL QDAARQVETA AAAMDGGDLE
TACIAAHSLK GAAGTVGADA LCEQALALEQ TARKGRVDEC VRRLSLLRQA LDRLAQDVAA
FLS
//
