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Database: UniProt
Entry: A0A0C3RDD9_9PORP
LinkDB: A0A0C3RDD9_9PORP
Original site: A0A0C3RDD9_9PORP 
ID   A0A0C3RDD9_9PORP        Unreviewed;      1065 AA.
AC   A0A0C3RDD9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BA92_12900 {ECO:0000313|EMBL:KIO42769.1};
OS   Sanguibacteroides justesenii.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Sanguibacteroides.
OX   NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO42769.1, ECO:0000313|Proteomes:UP000031980};
RN   [1] {ECO:0000313|EMBL:KIO42769.1, ECO:0000313|Proteomes:UP000031980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO42769.1,
RC   ECO:0000313|Proteomes:UP000031980};
RA   Sydenham T.V., Hasman H., Justensen U.S.;
RT   "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT   genome.";
RL   Submitted (JUL-2014) 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:KIO42769.1}.
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DR   EMBL; JPIU01000049; KIO42769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3RDD9; -.
DR   Proteomes; UP000031980; Unassembled WGS sequence.
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; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031980};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          427..468
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          703..915
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          944..1057
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         992
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1065 AA;  122808 MW;  F67057E1EACE4B63 CRC64;
     MDRILTDLKI GWWKVDHEKK GYVLSDIAVK MLKLDSNIIR FKTFTEMIRE DYRARIMKEI
     ENIENQYLYD QTFPIQTPSG EIWLRSKIIH KETDEKGNSS ISGFIQIIPN PEVTQPEKAS
     LLRINNLLYQ LNTISHTLLS FLQSDTADTV INKILENILE QFKGGRAYII EYNWEKKTQT
     CTYEVTDSNV NKEQSRINDM PMEESPWWTR QITRQKHIIL SDLNELPEEA YIEKEFLALQ
     EIKSIIVAPL ISHEGVWGYV GIDVVEEHHE WSNEDCQWFT SLANIINICI GLQRSEHEAQ
     IDRTYLQNLY KHMPLGYTRL KLLYDSNRQP IDYLFVDANY AAGEINGYNV EKYIGHKASE
     LRVNLKEELV YLQDILHTKK HADVNYYIEP LKKHCHAIIY STVEDEVICL ISDITESYNT
     HEALDRSEKI LRNIYDNLPA GIELYDKTGK LVDMNIKDLE IFGLKRKEDA LGVSIFENPN
     IPAEIIEKIR KEEPVSFRLN YSFKSIEHYY SSTKKGNIEI YTTVSALYDK QGNLIHYLFI
     NIDNTEISNA YSKIAEFESS FSAISKFGKI GYCKFDLFTK NGYGVAQWYR NLGEHETTPL
     PQIIGVYNHV HEEDKAYILD SIRKVKAHET DNFSRDLRVH TEEGWKWTRI NVMRNTMNND
     TGKLEMLCVN YDITELKETE KKLIEAKNRA EISDRLKSAF LANMSHEIRT PLNAIVGFSN
     LLTETDDRDE RAAYFDIVQE NNELLLQLIS DILDLSKIEA GTLDITNSDV NVNQLCEEII
     RSFSLKAEEN NIEILFEQHL PACHINSDKN RLTQIITNFI NNALKFTSKG SITLGYYQSG
     PEEIKFYVKD TGTGIPKDKI NNVFERFIKL NSFAQGTGLG LSICKSLAEQ MGGEIGVESQ
     EGKGSCFWFT HPFHPDVQLK LSFETTEIKA IEPAHLFPNP SQPTILVAED TDSNFLLVSA
     ILKKDYRLFR AVDGVEAVKL AAEIHPDLIL MDIKMPHMDG IEATKEIRKT DKNVPIVAVT
     AFAFDSDRQR VLDAGCNDYM SKPITGPELH QKLREMIRLR FKKTP
//
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