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Database: UniProt
Entry: A0A1I4BFQ6_9PORP
LinkDB: A0A1I4BFQ6_9PORP
Original site: A0A1I4BFQ6_9PORP 
ID   A0A1I4BFQ6_9PORP        Unreviewed;      1344 AA.
AC   A0A1I4BFQ6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216357_104198 {ECO:0000313|EMBL:SFK67712.1};
OS   Porphyromonadaceae bacterium KH3CP3RA.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX   NCBI_TaxID=1855396 {ECO:0000313|EMBL:SFK67712.1, ECO:0000313|Proteomes:UP000198708};
RN   [1] {ECO:0000313|EMBL:SFK67712.1, ECO:0000313|Proteomes:UP000198708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH3CP3RA {ECO:0000313|EMBL:SFK67712.1,
RC   ECO:0000313|Proteomes:UP000198708};
RA   de Groot N.N.;
RL   Submitted (OCT-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   -!- SIMILARITY: Belongs to the peptidase C25 family.
CC       {ECO:0000256|ARBA:ARBA00006067}.
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DR   EMBL; FOSU01000004; SFK67712.1; -; Genomic_DNA.
DR   Proteomes; UP000198708; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR013783; Ig-like_fold.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; 6.
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; 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; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Kinase {ECO:0000313|EMBL:SFK67712.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transferase {ECO:0000313|EMBL:SFK67712.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        776..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          834..1049
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1091..1206
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1238..1337
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1139
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1344 AA;  153541 MW;  EC38CE0BC5074D6E CRC64;
     MQTILFIFFI FWISCLKSFS IELNFKYYKV EDGLSSNTVY AVLQDSRGFM WFGTENGLNR
     FDGYTFTAYR NTPRNENSLI NNYVYCLIED GDQTLWIGTE RGVCTFDLGK DGFNPFILKT
     EKGIQVSGRI QNLVPDNGKI WITSARQGVF VYENNKLSLH SFEEFKTNPD EQIWVTGIYK
     DKENIIWASV DNTGHQIYRF NKESGKFTPG FPDMCFDEQK QLRAYSMLED TFGTLWFGTW
     TNGLIAVDKN KGIITERHLH IPGKGKILHI HQLTEYDPGT ILIGSNDGLT SFKISPIAGN
     RPDQHFREPK LSNCFVYPIY KDNEGGLWIG TYHGGINYAS PNRNYFTGYT HSRYENSITG
     NVVSCFCEDP SGNIWIGTED GGLNELEVKT GKFQAYSYKD ETDGLSFDNV HALLIDNDQL
     WIGTYTGGLN VMDLRTKKIK HYVSDHADKN SLDANNIYSL YRDSLENIWI GTTSGINVYN
     RQSDNFTRVR NLNEIVMDIL QTGKHIWFAT INRGLQKLNL ESGKWTEYTF EYDNEHSLIS
     NDVISLCIDE EQQLWIGTNH GLCRYDAEKD IFIDEKVEFQ SNYICKIFAE NGNLWIATLK
     GLICYTPSTR QYRQFTKSDG LLSDLFTPNS GFKSSSGKIY LGTPNGFNTF YPKQIPKNMH
     VPLIAITDFQ LFNKPVNMDG FVAENKQNQS VLTLAHNKNS FSFGFTALSF FAPEKNRYMF
     MLEGFDKSWN DAGKERRATY TNIPPGNYMF RIKASNNDGV WNDEDYTLAI IIKPPLWWNG
     WSITFYILFV TAGIVYLFRF LREKDRRKNE EKIAKIRSEQ EKETYRSKIE FFTNVAHEIR
     TPLSLIIAPL EQIIETSDTM SDAITENLDI MRSNSQRLLT LVNQLLDFSK IEKGGIQISL
     SNQNIHHLLA EIYQRFKPFI EHKHILFEYI CDDTDFETMT DAENLTKVVS NLLSNASKYT
     TDHILLKLNA HLSADYYEIS VKDNGAGLSE SETEHIFKPF YQAPGQYNSG TGLGLFLVKS
     IVDALDGKIA LINNPGESFS ISVVLPKINR QVEYPPPGEY STETQMSSGI EPESCDSGNI
     CCDSGNDEKP SLLIVEDDKD MQAFIRKQFQ NNYLVYTAND GNEGIDILEN HPIDIIVTDM
     MMPNMDGITF CKTVKQNFLW SHIPVIMLTA RTNVGSKIEA FETGADAYLD KPFHISYLSA
     RIRNLLESRR LLFQKFSQTP HASLKSIAGN KTDEDFLVKL NEIIEKNIEN SDFSIDNLAK
     EMGISSSGLF AKIKQISGVT PNKLILSMRL KKAAGLLSGG RYRVNEVCYR VGFNNPSYFA
     KCFQKQFRKL PKDFISDPDE KTED
//
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