ID A0A1I1TAL7_9BACT Unreviewed; 1393 AA.
AC A0A1I1TAL7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05518672_102411 {ECO:0000313|EMBL:SFD55661.1};
OS Chitinophaga sp. CF118.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFD55661.1, ECO:0000313|Proteomes:UP000199596};
RN [1] {ECO:0000313|EMBL:SFD55661.1, ECO:0000313|Proteomes:UP000199596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF118 {ECO:0000313|EMBL:SFD55661.1,
RC ECO:0000313|Proteomes:UP000199596};
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};
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DR EMBL; FOMK01000002; SFD55661.1; -; Genomic_DNA.
DR STRING; 1884367.SAMN05518672_102411; -.
DR OrthoDB; 1489484at2; -.
DR Proteomes; UP000199596; 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; cd00082; HisKA; 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; 3.
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; 5.
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 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 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:SFD55661.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:SFD55661.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1393
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011441080"
FT DOMAIN 903..1107
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1143..1258
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1290..1389
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1191
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1393 AA; 158369 MW; CBF5B750871B99A0 CRC64;
MRLQQWILLF LLLIAGHSYA QAISDPDSNI RLEQLTTRDG LSQNTIRCLL QDKKGFIWIG
TLNGLNRYDG RKFIVYRPEY GNPNSISDNR IRELHEDKQG LIWVKTIEGR FHCFDPRKES
FVEYLPDSVV KSYDHFFEAS NGEIWLYGKA NGSLRIRKQK KHFITQCYNK QQPVNFVSED
SRQGIWIGTT GGLFRLKNDE QEIVFRGNFI QAITDQQQVY FITRQSGIFT LAGQQFNIPE
GIQLTNAALL AGSRLLLGTQ QSGVFVADLL SGQITPGNQL LGESITGHID VITDPQHRIW
INNHSGIVWY YDIIKQKTTR MELIPPAVMR LIDDCRYSFF SDNKHHTWIT TYGGGLYCYN
HVTDKLQHFS STPDNPNGLS SNYLLSILED RAGLIWVGAE HTGLNKLVPQ SLNVAHIFPE
ETSSGRYTAN SIKTIYEDSH DRLWVSTRNG ALYLYNSKLE KIRSLEHLLP GQCANIYCIT
EDTRGYLWIG TKGNGLYIVH RDSLQQRARH FELPAGDTSS NAYKLVYTIM QDQQQRMWIG
TFGSGLHLAV YKGGNNISFR QFFKNNEAPV YIRCLLQDKH NRIWAGTNNG LLVFDPEALM
HDEKAFTTYQ SNLKSKNGLA SNEIKTICED HKGRIWIGTT GGGFSQFMPR KRNFITYTTR
QGLSHDIVNG MLEDLQGNLW ISTENGVTRF NPEKRTFEIF YFANNTLGNL FSEAACSRTH
KGQLLLGSLN GFYSFYPEQL KTISADAAVI LTGLNIAGNQ RVNVTKEITL EPGQKIISIE
FASLAFKNPL QNKYTYILDK YEDEWNTPSS YNIATYRNLP PGKYKFRVRG TNDDGTWSKQ
EATIQINVLP PLWRSNPAIV LYLFILLALI LGIRYVTKRI SRLQHAVELE KQLTEYKLNF
FTNISHEFRT PLSLIMSAME SMSPGKHLHM MQKHVTYLMR LADQLLDFRK IQHKKMQLQV
QQTDVISFLR DICDGFNDQA AQKQISLDFH SNVSTYSMWI DTNKLDKMLY NLLSNAFKFT
PAGGHVVVQV RVADKLHILV SDSGISIPAA NQHLVFQKFT QLNFSPTGTG IGLSLTKELA
ELHKGNISFH NNPDAGVTFT ITLPLGNIYS PEETVPPEMT KAMMPAASIA ETEDIPIPSS
RYKVLIIEDN PDICEYLTTS LGRYFHIHTA NNGREGLAQA IAQAPDLVVC DVMLPEMNGL
EIVQRIRNEF QTCHIPVILL TALSSGEHQL KGIDAGADAY ITKPFSIRFL LTNIIRIIEQ
REKIRKRFAN DPGFFAVHIS ENEADQQFLD KLNSIIDKNI DNPQFSVDEF ATAMKLGRTL
FYKKIKGLTG YSPNEYIRLV RVKKASELLN TGEYTIAEVA YKIGMNDPFY FSKCFKAQFG
VPPSVHLKKL KTG
//
