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Database: UniProt
Entry: A0A1G1SWU7_9BACT
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Original site: A0A1G1SWU7_9BACT 
ID   A0A1G1SWU7_9BACT        Unreviewed;      1424 AA.
AC   A0A1G1SWU7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BEN49_13080 {ECO:0000313|EMBL:OGX83088.1};
OS   Hymenobacter coccineus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1908235 {ECO:0000313|EMBL:OGX83088.1, ECO:0000313|Proteomes:UP000177506};
RN   [1] {ECO:0000313|EMBL:OGX83088.1, ECO:0000313|Proteomes:UP000177506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8649 {ECO:0000313|EMBL:OGX83088.1,
RC   ECO:0000313|Proteomes:UP000177506};
RA   Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA   Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT   "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT   Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL   Submitted (AUG-2016) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGX83088.1}.
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DR   EMBL; MDZA01000422; OGX83088.1; -; Genomic_DNA.
DR   RefSeq; WP_070746312.1; NZ_MDZA01000422.1.
DR   OrthoDB; 9797097at2; -.
DR   Proteomes; UP000177506; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 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; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Kinase {ECO:0000313|EMBL:OGX83088.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:OGX83088.1}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1424
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009578470"
FT   DOMAIN          883..1115
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1158..1273
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1305..1404
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1206
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1424 AA;  158122 MW;  865404B5F59717CA CRC64;
     MQIPLVFRWL LVLWAGLLAP AAQAQDVALS DFRFEHITVD QGLSHSDAMA VAQDRAGFLW
     IGTNRGLNRY DGYSLKPYML ATNPRNGMSG NRITALLVGP DERLWVGTEL AGLSYYDAAH
     DAFRHFDEHA APPADQAAAR LLTESDVTVL TLDNQHHLWV GTIQHGIFVL TFGPQGRVLT
     LRQLPPTAAG RPALLRITSL AVDAERNVWA GTLGAGLVVI RTAEPAWPVE ATGFASKHIA
     SLCLDQRGDL WVGAERQVYW VPAANRRTGR ELAAHPLPQQ FPRIQALHLD SAGRLWVGTL
     YGLYVWEAGA PAGGALPLQA GRPTLFLPQD GEPFSINSER VHHIFEDRNQ TIWLCASAGG
     LNKVNLRQRA FGQLRRQLVG QLTLSNNYIN TIYKEEATNT LWFGTRNGVA AYNLVRHTYR
     NYFNQQEDAT RGVDVSTIFK AADGTLWFGT RSSGLLSLKR TGGREKLTRY TRLPTGFDLT
     STSIEHLAQD GEGTLWVATF SAGLLRLGPS GQYQGTYDMA RNHLPTNQFT HLLYDPARRV
     LWASTRNAGL LKLRPAPGAL TLLHQYQYAP GQPNGLDVNY VWPLLLDRQG ALWIGTIGGG
     LHQLRTDAQG HETMQSFVKY LPESDVESLL PDDAGNLWIG GTGLYRFTPS TRRYLRYDVA
     DGLQSNAFKI GAAARAQDGT LYFGGINGIN YFQPAAIQAN PTPPVVQLTG LRVMNRPVGV
     GQVFNGRVLL TKAFSEPQTV TIRAAENDFS VEFVALNYTN PQKNHYAYRL RGYNQDWVRP
     GPGQRTASFA NLPPGRYTLE VTADNGEGAW ARQLATMQFD VLAPWYKTGW AYLFYALVLL
     GVIVLYRRFE IAQQGLRNKL ALEQFQAEKE KELTNLKLGF FTNVSHELRT PLTLILGPME
     EIMGAPGPVS GMRDKVQLMH RQTRKLLDLV NQLLDFRKVE SGNVPLRASY GNAVPLLTDI
     FRAFEQKAAE RRLTYSLDVP AEAVPLYFDR SKLEIILTNL VANAFKYTPA GGRIELAATV
     VGSPGGEAVF EQDLLIGNYL EISVLDSGTG IRAEELGRIF DPYYQASHTD TLRMTGTGIG
     LSLVKQFAER HAGTIAVEST VGAGTAFRLR LPFGQAHLHP ADILPETEQP DALDNMSGFE
     ASELPLPSHP AAQTTRPRLL VVEDNDEVRQ YLQQLFEADY EVLAAADGQE GWEQVLARSP
     DLVVSDVMMP RSDGLELCQR IRQHPKTAHI PVLLLTARTA ALHEVEGLET GADDYVSKPF
     NPLVLQAKAA TLLRNRLKMR EFYQRQILLE PNEIVIADAD RAFLEQAMRA VEQHLEDPTF
     GVVVLANDLC LSQSVLYRRI KSITGQTTVE FIRDVRMKRA AQLLTHSQLR ITEIAFQVGV
     ENVKYFRKTF QKIYGMAPSE YAKQHRPDRE AVVAEGDALA TTDD
//
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