ID A0A444MIZ4_9SPHI Unreviewed; 1389 AA.
AC A0A444MIZ4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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=EPL05_21010 {ECO:0000313|EMBL:RWY48063.1};
OS Mucilaginibacter gilvus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2305909 {ECO:0000313|EMBL:RWY48063.1, ECO:0000313|Proteomes:UP000286701};
RN [1] {ECO:0000313|EMBL:RWY48063.1, ECO:0000313|Proteomes:UP000286701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F01003 {ECO:0000313|EMBL:RWY48063.1,
RC ECO:0000313|Proteomes:UP000286701};
RA Yan Y.-Q., Du Z.-J.;
RT "Mucilaginibacter antarcticum sp. nov., isolated from antarctic soil.";
RL Submitted (JAN-2019) 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:RWY48063.1}.
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DR EMBL; SBIW01000012; RWY48063.1; -; Genomic_DNA.
DR OrthoDB; 9809670at2; -.
DR Proteomes; UP000286701; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000286701};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1389
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019386412"
FT DOMAIN 871..1095
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1132..1247
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1279..1378
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1180
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1389 AA; 157567 MW; 5F65DEB78AFBC741 CRC64;
MRLKLYVSCV LCMLWQQQLF AQKDAYEFSR LDITNGLSDN QVNCIFKDEK GFVWFGTTSG
LNRYDGSKFK IFKRDNKNTN SLAENHVVRI EQGPDNKLWI FTHSNLSIYN PETEKISNNI
TAEASLYNIF TSYITHVRKD AAGRFWFITD NAGLYCYNPA NRSTFFYSTL PSSKARLHSS
NVMDVVITPQ NNVWLLYSDA FMEELNTGTN KITRRYDGFA KANSLRPSNY TLLLDNKSNI
WISSDGAPIG AFSYNTITNS LTHYSKDTPQ ARLNSNVINS IVQADDNKIW LGSDHGGANI
IDPKTNKVSF IMSKPDDAKS LSGNSLNLYK DNSGIIWAGT FKQGVNYYHS GIMQFPLFKH
FSSDPKSLPS GDVNTFAEDD KNNLWIGTNN NGLIYFNRAN NTFTQFKHNP ADANSIANDI
IIKLYIDKQH KLWIGTYFGG LDCYDGKRFT HYRHNPNDPG SIGDDRIYTI MEDHKGEMWV
GTFAGGYNVF DPKTNSFKHP KYSMNSEYTA IIYEDKDKNK WIGRDKGVDV IDYKTNKVRH
YLSQPKNLNS LVGNDVNAIT QDKRGLIWIG TKDGLSILDT KTNNFLNIEE GINLPANNVS
NIIEDKEGKM WVSTTNGLAK IQLSRVDGKY KFRINNYNEL DGLQGRAFNL YSALRLKSGE
LVFGGINGFN IFDPAIVNTF KPKPNLIFTD LHFFNKSVTV GDTVNGSVVL TKALSETKEL
TLAHNQNVFD IEFAACDYFN PDKIKFEYKL EGFDKGWITV AGNNRKATYT NLDGGDYVFK
VRTQNASLDD TISLNITVKP PFLKSPVAYV SYIVILVGGL LYIRHRGILK LKREFDTRQA
KMEAERKIAQ EREEARRMHQ LDLMKIKFFT NVSHEFRTPL SLILSPIDNL IKTTERPEQQ
NQLVTIKRNG KRLLNLVNQL LDFRKMEYNE LKLSLKKGDI VQFIKEVSSS FKDVAHQKQI
QFLVESDICS YVTDFDHDKI ERILFNLLSN AFKFTPSGGH ISVMLSMAGI NESPGAKNEL
EIKVIDTGIG IPKENQDKIF ERFFQDDMPE SLLNQGSGIG LSITREFVKM QGGTIEIESE
PDYGSCFTIS LPVGKQSELK DIKVVADNQT LESEPTIFKN PENTPGAGKK PTILLVEDND
DLRFYLKDNL KNSFHIVEAV NGKDGWQKAL AMHPKLIVSD ISMPVMNGIE LCKKIKADSR
TAEIPVILLT ALGTEEEQLA GLDSGANDYI IKPFNFEILL SKIHNSLRMQ TTFKKTYQKQ
IEVNAKGITV VSEDDKFLKN AFEYIELNIT NLNFSVEELA RHLNLSRVSL YKKLLTLTGK
TPVDCIRTIR LKRAVQLLEK SKLSIANVAY EVGFNNAAYF AKVFREEYGI LPSEYIAELR
NKEKEAELV
//
