ID M1WQ01_PSEP2 Unreviewed; 713 AA.
AC M1WQ01;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, 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 OrderedLocusNames=BN4_11464 {ECO:0000313|EMBL:CCH48699.1};
OS Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS (Desulfovibrio piezophilus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH48699.1, ECO:0000313|Proteomes:UP000011724};
RN [1] {ECO:0000313|EMBL:CCH48699.1, ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA Ollivier B., Dolla A.;
RT "The first genomic and proteomic characterization of a deep-sea sulfate
RT reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT piezophilus.";
RL PLoS ONE 8:e55130-e55130(2013).
RN [2] {ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; FO203427; CCH48699.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WQ01; -.
DR STRING; 1322246.BN4_11464; -.
DR KEGG; dpi:BN4_11464; -.
DR PATRIC; fig|879567.3.peg.1528; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_7; -.
DR Proteomes; UP000011724; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCH48699.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011724};
KW Transferase {ECO:0000313|EMBL:CCH48699.1}.
FT DOMAIN 9..164
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 285..338
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 351..575
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 594..710
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 645
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 713 AA; 79841 MW; EBC6ACE260D25BE3 CRC64;
MAEETRRFRV LAVDHDEEML TRYRDVLCFE GEEPAELEAL FNDDLQLPSQ EEIRAEANNP
IFEVIPCLSP EQALSTMANS LAKKNPFAIA LVEVHLGGRP TMAGIDLAEK IRALDHHIEI
VLLSSEASVP LKEINKRVCP PEKLLYVQKP FRSAELKQIA ASLCSKRDLE NRLYELNETL
TSKVEARTAE LNAVNRRLRL DIAKRASVLR ELQASERRYR MLFEKDITGN FAADGDGLIL
DCNGAFTTLF NFDSPQDAHG QDIFTLWDIM GASEPLHEII AGHHRVTNHE IVLRRGGINQ
HLLANFDTVF SEEGKLEELR GYIFDMSEPK RLEEQLRQSQ KMEALGTLAG GIAHDFNNIL
GVILGYAEII ESSAEPESGL ERRVREIARA GKRARDLVNQ ILNFSRQGPQ ERHPMTLTPL
IKEALKLLRS SMPTNVEIIS RMETDQDSVL ADPTQMHQIM LNLCANASYA MKARGGTLTV
TLTDASHGDE IFPSEGLGSP ERFVRLSVSD TGNGIPTDVV ERIFDPFFTT KKQGEGTGMG
LAMVHGIVKR HDGYLELENH LGQGATFHVF LPKTAMDERP VAEATSELVF REGRILFVDD
EKPLTDIGRE MLVACGFEVV TRTSSIEALE AFRHRAGEYD LVITDQTMPN MNGMELAREI
LKIRPDMPII LCTGFSDAVS YDRLRDIGIG DFIMKPILKH DLIASISRQL IGH
//
