ID A0A1F3MFC8_9BACT Unreviewed; 1305 AA.
AC A0A1F3MFC8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-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=A2X22_04665 {ECO:0000313|EMBL:OFY51407.1};
OS Bacteroidetes bacterium GWF2_49_14.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797354 {ECO:0000313|EMBL:OFY51407.1, ECO:0000313|Proteomes:UP000177245};
RN [1] {ECO:0000313|EMBL:OFY51407.1, ECO:0000313|Proteomes:UP000177245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY51407.1}.
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DR EMBL; MEOR01000087; OFY51407.1; -; Genomic_DNA.
DR STRING; 1797354.A2X22_04665; -.
DR Proteomes; UP000177245; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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; 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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..299
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 622..854
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 918..1031
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1040..1156
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1186..1302
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 571..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..102
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 967
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1089
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1235
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1305 AA; 146873 MW; 49ECD5621F63F830 CRC64;
MKTWFRNLKI KGKLNLMIGV SLLSLIIFGL TSVYLIKTTK VVNIMLIAQR DYMTDYHKSL
EYYYQFKQYQ ASGIIDRANI NLENAKNKIT SANDKLRLFS NVELILKKPN SVLIPEICNI
YGSAVGAVPG ETTTADARLL VNRMRLFGWL NLSAIKTSSE AANTALDLAE QILDVFVESE
SERITSGTTL TEKLSGILST MEREETAYAG SVKEISDTTI ISLKYTVIIL IIILGLLIYL
LSLAIGRLIT FPISSIRKNL NLMSKGDASG ISDYQSRDEI GQLADSYREM QSIMLGQVNH
ARKVANGDFD SLLEPRSEKD KLSLALNEMT RSLKASRVKS DHDNWIKSNQ NEMSFEIQGD
LDLDRLSQRI IGLISKQLDA LSGALFIFRN KKEVEFAAGF AVNTDQASKR SFKPGDGLIG
QAMKDKKPIL VKDVPGGYLD IYSGTGSTRP KHLLIVPCIY NSVTEAVLEL GSVKPFNPAS
LEYLNLVAES IAIAMQASKS RTELQNLLEK QEKMTEELQV QQEELRQTNE ELQVQQEELR
QANEELETQT RELEESKSNL QAQQEELRVT NEELAERSRA IESQKDSLKR KNDELEKARQ
DIEEKAREIE QVSRYKSEFL ANMSHELRTP LNSILVLSQI LSQNKDNNLT EKQIKSAQTI
KSSGENLLVL ISEILDLSKI ESGKVELHTE NVEISSVVQD LFETFHSMAE VRKLAFETAI
DEDIPLHIQT DSLRLGQIMR NLISNAIKFT ETGFVKLRVC RPLKPEQLPA RFQGRKDLIG
FYVEDSGIGV AKEKQKEIFD AFKQADGTTT RKFGGTGLGL AISRNFSRLM GGDILLDSQT
GKGSLFILLL PEASSVLKGP GLAIHQIVHE NPEAEFKMQE IPAQKQEKVP FSEPAEEMWI
EETSVLDDRK EIKKGDTFLL IIEDDNSFAQ IVLDLAHEKN FKCMIAPNGE TGLHYADYYS
PSAIILDIGL PGIDGWEVMK RLQENPATRH IPVHFMSGTD KSLEALKKGA IGFLTKPVTI
DEINEAFDRI EGLISKPLKK LLVVEDDAAM RLSIHELIGE ENIQIVSVSK GQEAIELLKK
ESFDAMILDL GLEDMTGYDL LQKIGKRKDS HAMPVIIYTG KELTREEEER LKSYSDRIII
KGIKSPERLL AETTLFLHQV QSNLPEEKQK MLRNLHPKED VMKDKIVLIV DDDMRNVFAV
TSLLEDVGLK IVVGKNGRDG IEKLKNNPVD LILMDIMMPE MNGYEAMEEI RKEMKYRKLP
IIALTAKAMP GDREKCLRAG ASDYLTKPID SEKLLSMLRV WLYKG
//
