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Database: UniProt
Entry: A0A1C2GJ48_9SPHI
LinkDB: A0A1C2GJ48_9SPHI
Original site: A0A1C2GJ48_9SPHI 
ID   A0A1C2GJ48_9SPHI        Unreviewed;      1360 AA.
AC   A0A1C2GJ48;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BEL04_16145 {ECO:0000313|EMBL:OCX51554.1};
OS   Mucilaginibacter sp. PPCGB 2223.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX51554.1, ECO:0000313|Proteomes:UP000095113};
RN   [1] {ECO:0000313|EMBL:OCX51554.1, ECO:0000313|Proteomes:UP000095113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX51554.1,
RC   ECO:0000313|Proteomes:UP000095113};
RA   Seilhamer J.J.;
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:OCX51554.1}.
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DR   EMBL; MDJS01000003; OCX51554.1; -; Genomic_DNA.
DR   RefSeq; WP_066005822.1; NZ_MDJS01000003.1.
DR   STRING; 1886027.BEL04_16145; -.
DR   OrthoDB; 9809670at2; -.
DR   Proteomes; UP000095113; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   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; 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; 9.
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; 4.
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:OCX51554.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000095113};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:OCX51554.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1360
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008661845"
FT   TRANSMEM        799..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          853..1073
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1114..1229
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1261..1360
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1162
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1360 AA;  154333 MW;  2B1ED23BAEF7059B CRC64;
     MKKFLLFIIL QLVLISPSFS QLSFDHVSVN NGLSQSTVLT ILKDSRGYMW FGTRDRLNKY
     DARNIKTYNY DYRDTTSISC NDYVFFVFED RQKNLWIGTS KGLNRYIPES DSFERILHKD
     NDRNSLTTNN IYCTYQDHSG KLWFGSDKGL NMLSSPASRK FTRFFKASPG HPGLSGNQVY
     AIYEDREQNL WVGTTEGITR MSLKNGKYIF KTFNSANGLE GNFVQTITQD HEGNICIGTQ
     TGGVNIFDPK TATFSHLKHN PSNTNSLINN DIRKIVIDKD DKLWIGTMNG LDIYDQHSRQ
     FKLYQHDVEN RNSLSDNSVK DIYFEDNGTV WIGTMFGGVN IIHPNTVPFN IYQASKYKNS
     ISGNVVSTII ADAKQNLWIG TEGNGLNYYD KAKLTFTHYT NNPNAEGSIR TNFVKAIYRD
     KANNLWVGLH QGGLELLQPS SGTFKHYRHN DADPHSINSD IISCILEDSA NRFWVGTSKG
     LDIFDQKQQQ FRTYLNDPSK PLKLSSIGIR CIYEDSGHNI WVGTSGGLNL LKAGTTSFIF
     FRANDRDEKS IKAGYINCIR QDNDGNIWVG SFHGGLSRYN PGDGSFKTYQ IKDGLLSDNV
     LNIIPADAHD LWISTNNGLT KFNTLTQKFK NYTVADGLPT NEFNYNSSYK DADGILYFGT
     YNGLISFDPK QIKENKVTPA VLFTGLKLFN HPVNISDQTG LLQKHISLTK AIIFRSDQNV
     FTLDFTALDY DKPGENQFMY KLKGFEKNWN VVDVPSATYT NLPAGDYDFL VKASNADGYW
     NNNTTGLHIV ILPPLWRTWW AYTFYVLAFA GSLFLVIRFF RRQARLERDL YYEHLNYERQ
     QEVHQMKLDF FTKVSHEIRT PLTLILAPVE KLIDTTLDNP LVSRQLTYVK QNADRLLRLV
     NELLDFRKIE TGHLQLHVSE HDLIRFCEDI FSSFERTSIQ KSITYQFKPA IDSLPLYFDP
     AQFEKVLFNI LSNAFKFTPD EGTITLSVTA DAQWVNIIIA DNGAGIAAEQ QAHIFENFYQ
     ARNNTTSPGW GIGLALVKNI VDQHKGKISV ESELATDAQP GKTVFTISLL KGKAHFDAAD
     LDDTPAQSYA IQQAVATPVM ANTESLSPIA EKQSILLVED NNEVRGLIRE SLATSYNIHE
     SINGAEGWET ACQLIPDLII SDVTMPVMDG LEFCSKIKTD ERTNHIPVIL LTAKAAYDHQ
     VSGLENGADV YITKPFKMQL LELTIRNLMM TRQSMREKFG QQITLMPKNK VIESPDEKFL
     NKLMTIVETH MEDSEFDVVK LVNEIGMSQS ILYRKIKALT DLSTGDFIKS VRLKQAALLL
     AQQKLSIAEV AYAVGFSDRK YFSKEFKKQF GKTPSEYIEQ
//
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