ID A0A0E9MVH6_9BACT Unreviewed; 2032 AA.
AC A0A0E9MVH6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FPE01S_01_05980 {ECO:0000313|EMBL:GAO41584.1};
OS Flavihumibacter petaseus NBRC 106054.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO41584.1, ECO:0000313|Proteomes:UP000033121};
RN [1] {ECO:0000313|EMBL:GAO41584.1, ECO:0000313|Proteomes:UP000033121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO41584.1,
RC ECO:0000313|Proteomes:UP000033121};
RA Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., Ohji S.,
RA Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC 106054.";
RL Submitted (APR-2015) 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:GAO41584.1}.
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DR EMBL; BBWV01000001; GAO41584.1; -; Genomic_DNA.
DR STRING; 1220578.FPE01S_01_05980; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000033121; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 10.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 7.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 8.
DR Pfam; PF18947; HAMP_2; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 11.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 5.
DR PROSITE; PS50885; HAMP; 11.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000033121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 140..197
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 237..289
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 329..381
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 421..473
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 513..565
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 605..657
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 697..749
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 789..841
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 881..933
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 973..1025
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1065..1117
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1357..1590
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1649..1762
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1913..2030
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1091..1118
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1288..1347
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1698
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1963
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2032 AA; 221435 MW; AA44F229F926F82D CRC64;
MATRKSSPQK ETRTLPPSPK KVVKASGTNG TTSTITKPKS HVLPAFEDDV LNANELLTVL
SEVKNGNFAI RMPFNKLGTS GKICDVLNEI ISLNEILMQE LSLARNTIGK EGKLNHRVEL
PRAARGEWRN GVNSLNTLIS DLVHPTIEIA HVISSVAKGN LSQEMPLKIG DHGLQGEFAR
IATEVNDMVK QLNLFSMEVT RVAREVGSEG KLGGQARVKG VAGVWKDLTD SVNQMAGNLT
AQVRSIAEVT TAVAKGDLSK KITVDVQGEI LELKNTINTM VDQLNSFSSE VTRVAREVGT
EGKLGGQAEV QGVAGTWKDL TVSVNQMAGN LTAQVRNIAD VTTAVAKGDL SRKITVDVKG
EILELKNTIN TMVDQLNSFS SEVTRVAREV GSEGKLGGQA TVKGVGGVWK DLTESVNQMG
SNLTAQVRNI ADVTTAVANG DLSKKITVDV QGEILELKNT INTMVDQLNS FASEVTRVAL
EVGTEGKLGG QAKVQGVGGT WKDLTDSVNQ MGSNLTAQVR NIAEVTTAVA NGDLSKKITV
DVAGEILELK KTINTMVDQL NSFASEVTRM ALEVGTEGKL GGQATVKGVG GTWKDLTDSV
NQMGSNLTAQ VRNIAEVTTA VAKGDLSRKI TVDVKGEILE LKNTINTMVD QLNSFGSEVF
RVAREVGSEG KLGGQADVPG VEGLWKDLTD SVNIMASNLT SQVRNIAEVT TAVANGDLSR
KIEVDVKGEI LELKNTINTM VEQLRAFASE VTRVAREVGT EGKLGGQANV PGVAGTWKDL
TDSVNQMAGN LTAQVRNIAD VAIAVANGDM SRKITVDVRG EILQLKETLN TMVDQLRAFA
SEVTRVAREV GTDGKLGGQA FVPGVAGTWK DLTDSVNQMT GNLTSQVRNI AEVTKAVASG
DLSKKVTIDV KGEIFDLKNT INTMVDQLNS FAFEVTRVAR EVGTEGKLGG QSEVQGVAGT
WKDLTDSVNM MASNLTNQVR GIAKVVTAVA TGNLKQKLSI VSRGEVAQLT DTINEMIDTL
ALFADQVTTV AREVGVEGRL GGQASVPGAS GIWKNLTENV NQLAENLTTQ VRAISEVASA
VTKGDLTQSI NVEAKGEVEE LKDTINQMIT NLKQTTLRNQ EQDWLKSNLA KFTQMLQGQR
EINTVTKRIL SELAQVVNAQ KGMFYILQED ENTAEQKLKL FASYAYDDAL SLNREFSLGE
GLVGQCAVEK QPILISNVPA NYIKIGSGLG ASDPVNLIVL PVLFETNIKA VIELASFEPF
NQTHLDFLNQ LTESLGVVLN TIEANSRTER LLGQSQSLTD ELRRANEELQ DKAHLLAKQK
EEVENKNQEV EEARVSLEEK AEQLQLTSKY KSEFLANMSH ELRTPLNSLL ILAQQLYENA
EGNLTDKQVK YAKTIHSCGD DLIQLINDIL DLSKIESGYI STDFINIHFA EIVSFVESTF
KHVSENKNLR FIIEKDRNLP DIIETDSQRL NQILKNLLSN AFKFTEKGEV RLRIYEADHE
WLQPNDNLDN ARRVVAFEIR DTGIGISKEK QNIIFEAFQQ AEGSTSRKYG GTGLGLSISR
GLAELLGGSI ELVSEAGMGS TFTLYLPLEP GTIPTKKEKG SLRKRSEYAV GETLVPTIKV
SDTKELESLN EIINDNGDDR NNINADDLVI MVVEDDLQFA HIILEVAHTT GIKVVIATNF
AAVFELANRF SLAAITLDVK LPDASGWRIL DLFKNDDNLK HIPVHVISGE ENRHLARQRG
AKNFHLKPIS GTELNSMLQE IRTFHQRPLR NVLILSDRDT HLLAEKLQEP GLLEFITTSN
AETAMDTISK QPIECLVLDH EAADPTPQEA YADLLDLAGK LNIPVILFTP PGEAVNAWLK
SVSQVITKAD GETGVLLHEL IGYSHVNLKQ LSADKTGMVE KARMKKDILN QKNILVVDDD
VRNLFALTTA FEKYNINSIT AESGMEAMEL LGQPNQIDMV LMDIMMPEMD GYETIQKIRR
EHKNNSLPII AVTAKAMKGD REKCLEAGAS DYITKPLKID QLLSLMRIWL HK
//
