ID A0A1M3H9W6_9SPHI Unreviewed; 1903 AA.
AC A0A1M3H9W6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BGO55_18440 {ECO:0000313|EMBL:OJW55147.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW55147.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW55147.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW55147.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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};
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:OJW55147.1}.
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DR EMBL; MKTZ01000020; OJW55147.1; -; Genomic_DNA.
DR STRING; 1895841.BGO55_18440; -.
DR Proteomes; UP000184242; 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; 9.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 2.
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; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
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; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 10.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
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; 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OJW55147.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 83..140
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 180..232
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 272..324
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 364..416
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 456..508
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 548..600
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 640..692
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 732..784
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 824..876
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 916..968
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1215..1448
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1516..1629
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1638..1753
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1783..1901
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 942..969
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1146..1205
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1565
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1687
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1834
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1903 AA; 208222 MW; 7A4AD687068453B1 CRC64;
MRILMQVRNG NFSVRMPIDE TGIKGKICDT LNEIISLNEE MMREFTKAGN TIGKQGKLTQ
RIEVPNAKGS WATGVDSLNS MISDLVHPTI EIAHVISSVA KGNLSQNMPL EIGGHTLQGE
FSRIAREVND MVKQLNLFSM EVTRVAREVG SEGKLGGQAK VKGVAGVWKD LTDSVNLMAG
NLTAQVRNIA DVTTAVAKGD LSKKITVDVK GEILELKNTI NTLVDQLNSF SSEVTRVALE
VGTEGKLGGQ AHVRGVGGTW KDLTDSVNAM ASNLTGQVRN IAEVTTAVAK GDLSRKITVD
VKGEILELKN TINTMVDQLN SFSSEVTRVA REVGSEGKLG GQADVPGVGG TWKDLTDSVN
IMAGNLTAQV RNIAEVTTAV ATGDLSRKID VVVKGEILEL KNTINTMVDQ LNSFSSEVTR
VAREVGSEGK LGGQAAVEGV GGVWKDLTDS VNQMAGNLTG QVRNIAEVTT AVAKGDLSRK
ITVDVRGEIL ELKNTINTMV DQLNSFGSEV TRVAREVGSE GKLGGQADVP GVGGTWKDLT
DSVNKMAGNL TAQVRNIAEV TTAVANGDLS RKITVDVQGE ILELKNTINT MVDQLRGFAS
EVTRVAREVG TEGKLGGQAF VPGVAGTWKD LTDSVNQMAG NLTAQVRNIA EVAIAVANGD
MSKKITVDVR GEILQLKETL NTMVDQLRAF ASEVTRVARE VGTDGKLGGQ AFVPGVAGTW
KDLTDSVNSM TGNLTAQVRN IAEVTKAVAS GDLSKTVAID VKGEILDLKN TINTMVEQLN
SFAFEVTRVA REVGTEGKLG GQAEVRGVAG TWKDLTDSVN MMASNLTNQV RGIAKVVTAV
ATGNLKQKLS IVSRGEVAQL TDTINEMIDT LALFADQVTT VAREVGVEGR LGGQASVPGA
SGIWKNLTEN VNQLAQNLTT QVRSISEVAS AVTKGDLTRT IRVEAKGEVE ALKDTINQMI
ANLKETTLRN QEQDWLKSNL AKFTQMLQGQ KDLNTVTQRI LSELAQVVIA HYGAFYILKQ
DEDTRVDKLR LFAAYGYRAE KNIPTEFFMG EGLVGQVAFE KERIILSNVP SNYIKISSGL
GRAKPANLII LPVLFENKVK AVIELASLDV FSETHLDFLS QLTESIGIVL NTIEANTRTE
ELLAQSQSLA GELKIQQEEL RRTNDELQDK ALLLVKQKNE VEAKNKEVEE ARRSLEEKAE
QLTLTSKYKS EFLANMSHEL RTPLNSLLIL AQQLYENAEG NLTDKQIRYA KTIHSCGDDL
IQLINDILDL SKIESGFITA NISPVRFGEI ASFVETTFKP ISEARHLRFT IETDPRLPQS
METDLQRLNQ ILKNLLSNSF KFTEKGEVKL KIYQADNNWK QSNPNLDGAE KVVGFAISDT
GIGIPQEKQN IIFEAFQQAE GSTSRKYGGT GLGLSISRGL AELLGGTIEL ESAPGRGSTF
TLFIPIENVA GIISKETSDN LNAYQQLQLG GDSGEIDTLL NSLRVTNEDG GKMNIVSEMI
NDTGDDRHNI QSGDKIVLIV EDDLRFGKII IEKAHLYGIK AVVATNYIEV FDFINRFTPI
AITLDVKLPD TSGWKVLDLL RNDLNYRHIP IHLISGEENR TLALRRGARS FLLKPLENDA
LNELLDDIVT FAGKQTRKVL VVEDNEVDYS QITRMLQGDN IDVTLATTGR KALQDTNIKE
YDCIILDYTL PDISGIDLIT QVSESKKKLT PVIVYSAKDF DKKELYHLNR TSNTVLLKGV
NSLEHLLEET VLQLHINHKD LPIEKKRVIE HIRMKDDILT GKNVLVVDDD VRNLFALTTV
FERYNINVIT AESGREAINI INDDRQKIDM VLMDIMMPEM DGYETTQKIR REHKNSTLPI
IAVTAKAMKG DRQKCIEAGA SDYITKPLKI DQLLSLMRVW FYK
//
