ID A0A1I0RAB4_9BACT Unreviewed; 1369 AA.
AC A0A1I0RAB4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05428988_4700 {ECO:0000313|EMBL:SEW37657.1};
OS Chitinophaga sp. YR573.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW37657.1, ECO:0000313|Proteomes:UP000198758};
RN [1] {ECO:0000313|EMBL:SEW37657.1, ECO:0000313|Proteomes:UP000198758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR573 {ECO:0000313|EMBL:SEW37657.1,
RC ECO:0000313|Proteomes:UP000198758};
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; FOJF01000002; SEW37657.1; -; Genomic_DNA.
DR STRING; 1881040.SAMN05428988_4700; -.
DR OrthoDB; 1489484at2; -.
DR Proteomes; UP000198758; 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 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; 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; 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; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1369
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011640753"
FT DOMAIN 879..1083
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1119..1234
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1266..1365
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1167
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1369 AA; 155308 MW; 69DBC62850325588 CRC64;
MRLHQWLLSC LLLLAGHSYA LAPSDPDNIR LEQLTTHEGL SQNTVRCLLQ DKKGFIWIGT
LNGLNRYDGR KFIVYRPNGI SDNRIRELHE DKRGLIWVKT AEGRFHCFDP EKETFLEYQP
DSLVKNYDHF FEASNGDIWL YGKANGSLHI QKKRQHFITH TYNKQVNFIF EDKGIWIGTT
SGLFRLDNGA LADAGKGNYI QAIKDQQQVY FITRQNGIFT LNGQHFVTPE HITNAALLPN
SRLLLGTQQS GVYIADLISG QTSPLLKDEI TGHIDIITDQ EKGIWINNHT GVVWYYDAAI
QKATRLELIP AAVIRLIDDC RYAFSADNKH HTWISTYGGG LYCFDKVSGN LQHFSSTPDK
STGLSSNYLL SILQDRSGLI WVGAEHTGLN KLVPQSLNVT HIFPEDESSG RYTINSIKTI
YEDSYNRIWV STRNGALYLY NSKLEKIRSL EHLLPGQCSN IYCITEDTKG YLWIGTKGNG
LYIVHRDSLQ QSARHFELPP GDTSSNANRL VYTIMQDKQQ RMWIGTFGSG LHMAVYKGGN
NISFRQFFNS NETPVYIRCL LQDKDNRIWA GTNNGLLVFD PEALLRSNTA FTTYSPGNEI
KTLCEDHKGR IWIGTTGGGF SRFKPKTRTF TTYTTQQGLS HDIVNGMLED LQGNLWISTE
NGLTRFNPEK STFEIFYFAN NTLGNLFSEA SCFRTHNGQL LMGSLNGFYG FYPEQLKTVS
ADAPVILTGF NIAGNQRVNA TGEITLEPGQ KIFSIEFASL AFKNPQQNKY TYILDKYEDE
WNTPSSYNIA TYRNLPPGKY TFRVRGTNDD GTWSKREASI QITVLPPFWR SNLAILLYLL
VLTALILGIR YVTKRITRLQ HAVELEQQLT EYKLNFFTNI SHEFRTPLSL IMSAMESMTP
GKHLHMMQKH VTYLMRLADQ LLDFRKIQHK RMQLRVQQTD VIAFLKDIYD GFTEQAAQKQ
ISLQFHSNVP SYYMFADVNK LDKMLYNLLS NAHKFTPAGG HIVVQIKVGD ELQIHVSDSG
ISIPPAKQHL VFQKFTQLNF SPTGTGIGLS LTKELAELHK GTISFHNNHD AGVTFTITLP
ITNEYTAEEI VSPDMTAVNI PAPYINETED LPIPSSKYHL LIIEDNPDIC EYLSTSLSRY
FHIHTANNGR EGLAQAIALA PDLVVCDVML PEMNGLEIVQ RIRSEFQTCH IPVVLLTALS
SGEHQLKGID AGADAYITKP FSIRFLLTNI IRIIEQREKI RKRFANDPGF FTVHISENEA
DQQFLDKLNQ IIDRNIDNPQ FSVDEFAAAM KLGRTLFFKK IKGLTGYSPN EYIRLVRVKK
ASELLNTGDY TIAEVAYKVG MNDPFYFSKC FKAQFGVPPS VHLKKVKAG
//
