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Database: UniProt
Entry: E6W0A1_DESIS
LinkDB: E6W0A1_DESIS
Original site: E6W0A1_DESIS 
ID   E6W0A1_DESIS            Unreviewed;       398 AA.
AC   E6W0A1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Selin_1589 {ECO:0000313|EMBL:ADU66319.1};
OS   Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC   Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC   Desulfurispirillum.
OX   NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU66319.1, ECO:0000313|Proteomes:UP000002572};
RN   [1] {ECO:0000313|EMBL:ADU66319.1, ECO:0000313|Proteomes:UP000002572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC   {ECO:0000313|Proteomes:UP000002572};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA   Bini E., Woyke T.;
RT   "Complete sequence of Desulfurispirillum indicum S5.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002432; ADU66319.1; -; Genomic_DNA.
DR   RefSeq; WP_013506200.1; NC_014836.1.
DR   AlphaFoldDB; E6W0A1; -.
DR   STRING; 653733.Selin_1589; -.
DR   KEGG; din:Selin_1589; -.
DR   eggNOG; COG3437; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_72_0; -.
DR   InParanoid; E6W0A1; -.
DR   OrthoDB; 9799273at2; -.
DR   Proteomes; UP000002572; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT   DOMAIN          11..129
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          186..398
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          139..170
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         62
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   398 AA;  45437 MW;  67544BC18B1D44B3 CRC64;
     MGTDERIRDM HILLVDDSTY NLALFETMLM DDGYTRISTA LNATSAYDLL ARHDDIALVV
     LDIIMPDIDG LEACRYIKSQ APLQDIPILI ATAKTDLETL QSAFDLGASD YVRKPLVNSI
     ELLARVRNLL NTQLELQLRR QGEEQLRKLN QELEERVQAE VEKNRQKDQV MLHQARLAEM
     GEMIGYIAHQ WRQPLNVVGL LCQEHYDHYC NGELSRDIME SGTTKILDQL EFMSQTIDDF
     RDFFRPDKSK SRFSIRHAIE TTLSLVGAAM EKNNIRVQVQ CDATPEVEGY PKEYAQVLLN
     IINNARDAII DNRVADPRIH IRVYTDHGKA VVSIHDNGGG IPDEIIEKMY YPYFSTKQEG
     HGTGLGLYMS KMIIERNMGG KIWARNRDGG AEFFVEMP
//
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