ID T1CQQ3_9PORP Unreviewed; 968 AA.
AC T1CQQ3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PORCRE_1884 {ECO:0000313|EMBL:GAD06162.1};
OS Porphyromonas crevioricanis JCM 15906.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1305617 {ECO:0000313|EMBL:GAD06162.1, ECO:0000313|Proteomes:UP000018031};
RN [1] {ECO:0000313|Proteomes:UP000018031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15906 {ECO:0000313|Proteomes:UP000018031};
RA Sakamoto M., Tanaka N., Shiwa Y., Yoshikawa H., Ohkuma M.;
RT "Draft Genome Sequences of Porphyromonas crevioricanis JCM 15906T and
RT Porphyromonas cansulci JCM 13913T Isolated from a Canine Oral Cavity.";
RL Genome Announc.1:e00483-13(2013).
RN [2] {ECO:0000313|EMBL:GAD06162.1, ECO:0000313|Proteomes:UP000018031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15906 {ECO:0000313|EMBL:GAD06162.1,
RC ECO:0000313|Proteomes:UP000018031};
RA Sakamoto M., Tanaka N., Shiwa Y., Yoshikawa H., Ohkuma M.;
RT "Draft Genome Sequences of Porphyromonas crevioricanis JCM 15906T and
RT Porphyromonas cansulci JCM 13913T Isolated from a Canine Oral Cavity.";
RL Genome Announc. 1:e00483-13(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: 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:GAD06162.1}.
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DR EMBL; BAOU01000062; GAD06162.1; -; Genomic_DNA.
DR RefSeq; WP_023938656.1; NZ_BAOU01000062.1.
DR AlphaFoldDB; T1CQQ3; -.
DR Proteomes; UP000018031; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; cd00075; HATPase; 1.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF00072; Response_reg; 1.
DR Pfam; PF13424; TPR_12; 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 SMART; SM00028; TPR; 6.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
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 Lyase {ECO:0000313|EMBL:GAD06162.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..675
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 710..825
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 862..963
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 758
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 968 AA; 110058 MW; 355EE4627324267F CRC64;
MQHRIAQHIV FSGIFSSPLQ FIAREERSFC ILRSTLSIFL IFYILSIVSC EKKDSSALSS
EERIAIENRV ANIHETDSLA SLQKRLENEG NRLGSIIALR KWGKALRNEN RFDEALRVHS
EGVKQAEALG DTIEWVRGLN NIGTDYRRMG VIDAAQEYHY QAWILSRESM DKSFATKKNQ
VVSLNGLANI YMTLGNYQQA DSVLRLALAG EQQLGNVVGQ AINCANLGAI FEQQGQTDSA
WIYYRRSMDL NKQAGNRLGV SLCHTYFGSL YEKAHQHNEA LQEYETAYEL MQGSKDEWHA
LNPLIALAGI HSTKGNNTET LKYLSQAKAV AERINSKEHL AEIYNLYYGY YERQQDYQQA
LKCRNRAVTL QDSVVNIEKM NRIQNVSLNI ERKYQKQQID AAQMKLVAER ETRRIGYIIF
VLILSFLVII IAMMYYIQRI RARNHRALKE MNRLRESFFT NITHELRTPL TVILGLSHNL
QVDRTLSDKT REKARIIERH GNSLIVLINQ LLDIAKVKST VGSAEWRRGN ISAHLAMIVE
TYREYARSHN IVLQFFSEEA VEMDFVPDYI NKVMNNLLSN AFKFTPKYGK VNVAMRCEGK
RLLIDVSDTG AGIAPDAIAH IFKPFYQAES NTPNIGSGIG LALVKQIVDA IGGSISVESC
IGRGTTFHLD LPIHLNSKQQ IANETERNIP LLPQEKTALD DDREKDNECR LLIVEDNRDV
AAYIGSQLSD RYAISYAHNG NEGLEKALSL VPDLIISDLM MPGMDGLELC KQIRDNEIVN
HIPIIVVTAK VSEEDRIKGL EAGANAYLAK PFNSEELRTL VEKLLERQKL LREKFARTII
ESKDQNKESN GLQANIDFRF LAKVSETVYL MLSSRQEVDV SLIASKLCMS NSQFYRKMTS
LTGYTPMAYI QRIKIKKVCR LLDNDPEISL REAAEQCGFN DYSNFIRAFK NVYGITPSDY
RKGQLSML
//
