ID A0A1M4SBS9_9BACT Unreviewed; 1371 AA.
AC A0A1M4SBS9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05444008_10163 {ECO:0000313|EMBL:SHE29632.1};
OS Cnuella takakiae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Cnuella.
OX NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHE29632.1, ECO:0000313|Proteomes:UP000184368};
RN [1] {ECO:0000313|EMBL:SHE29632.1, ECO:0000313|Proteomes:UP000184368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26897 {ECO:0000313|EMBL:SHE29632.1,
RC ECO:0000313|Proteomes:UP000184368};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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};
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DR EMBL; FQUO01000001; SHE29632.1; -; Genomic_DNA.
DR RefSeq; WP_073038906.1; NZ_MTFE01000010.1.
DR STRING; 1302690.BUE76_23175; -.
DR OrthoDB; 1489484at2; -.
DR Proteomes; UP000184368; 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; cd00063; FN3; 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; 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; IPR003961; FN3_dom.
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; 7.
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:SHE29632.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184368};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:SHE29632.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1371
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013155104"
FT DOMAIN 854..1077
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1120..1235
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1267..1366
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1168
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1371 AA; 153089 MW; AE1EC8B66063FC71 CRC64;
MFRKLALFCF CLIGHASLTR AQQDDINFTA ITTKDGLSSN TVNTILKDRY GQVWFGTEDG
LDKFDGLNLS IYRHIPGNKE SLPANEVLAL HEDQAGNIWV GTSGGSLSRY DRQYNRFVNY
PSAEQGISNS VIRGISSDNA GRIWVVHYDG VDILDPKTKK VEKLVLSPDG QGTTIFKDSR
QRIWIGTSAG LFRFQPGTKS LTRFVYTGNS STGLAGNQVN AITEDSSGNI WIGTSTGLSM
QRPGSAVFTN YRLDSNLTNG YNGNSINAIA VDGDKLWIGN STGLDIFQPR TGSITRLRQN
VRDIHSLNTS SVRYITIDKQ GIYWLGTTGG GVNKYDKNLN LFNLVRSNQF DPLGLNTSVV
TAFADGAGGQ VYVGTQGGGL SLYDPVNKIF RRVPLVSGRK NGSRYITILT LKKNRRGQLL
AGTYAEGLFV LDASGALYRQ LLQGNQPEDL NGNEIYSILE DRNGNLWVGT NGNGINILDR
DFKVIRRFTP TPRAPNDFLL PFNGYIRDLA EDRNGDIWIA THGGGIAQYN PGSGQFKIFN
TENSKLPNNK VQSLLMGSDG NLWAGTFGSG LALFNRATGQ FSVFSEKEGL PNSTIYKIVR
APEGTIWVST NKGISSIDPI KKVVHNYNYH NGLQNNNFIR GAGFLSANGT LFFGGLEGFN
YFNPKYLKRN ANVPQVLITD LKIANQSVTP GPDGPLRENI LVAKEINLDF KQNFTLSFVA
LNYTSPEQNQ YAYKLEGFDR DWIDAGHATS VSYTNLDPGE YRFRVRASNN DGIWNEKGTA
ITIIVHPPFW RSNYAYAFYL LAAIALVYYL RHRSMQKLKR KYLLEQERFH TEQERKQAMH
LHELDQLKIK FLTNLSHEFR TPISLILGPV DSLLQQEKNP QTNGQLRMVR RNAKRLLNLV
NQLLDFRKME EKELNLQLSE GELVSFIRDV ADSFRDLAER KRIDFVFRSG LDHFYTRFDQ
DKIERILFNV LSNAFKFTLE RGSIALILEP GGTTEAGTAS WVNIKISDSG VGISADKKDQ
VFDRFFQDTS AAAILNQGTG IGLAITREFV RLHGGSIAVD SELSKGTTFT IRLPFIPLET
PAATVPQDAD AALEEDSPEL APMPAEELVA AANGTTLLPT VLLVEDNEDF RAYLKENLQQ
HYKVFEATDG KEGWQKALAL HPQLVVSDIS MPYMDGIQLS QKIKSDKRTS HIPIILLTAL
TGEEDQIKGL QTGANDYITK PFNYGVLHAK INNLLVLNDT LKHTYSKQLK VATPDIELES
DDERLLKDIM AYLEENLTNP QLSVEELSRN IGMSRSSLYN KLLEITGQTP VEFIRSVKLE
KAAVLLEKSD MTIAQIAYSV GFSTPNYFAK TFKTKYNMLP SEYITQRRKT N
//
