ID F5RDX2_METUF Unreviewed; 641 AA.
AC F5RDX2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=METUNv1_02489 {ECO:0000313|EMBL:EGK71103.1};
OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK71103.1, ECO:0000313|Proteomes:UP000005019};
RN [1] {ECO:0000313|EMBL:EGK71103.1, ECO:0000313|Proteomes:UP000005019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC {ECO:0000313|Proteomes:UP000005019};
RX PubMed=21725020; DOI=10.1128/JB.05331-11;
RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT representative of the order Rhodocyclales.";
RL J. Bacteriol. 193:4541-4542(2011).
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:EGK71103.1}.
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DR EMBL; AFHG01000052; EGK71103.1; -; Genomic_DNA.
DR RefSeq; WP_008062116.1; NZ_AFHG01000052.1.
DR AlphaFoldDB; F5RDX2; -.
DR STRING; 1000565.METUNv1_02489; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 6114847at2; -.
DR Proteomes; UP000005019; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
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; 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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-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; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005019};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..249
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 282..495
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 516..633
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 234..268
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 567
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 641 AA; 69012 MW; 78BD3C04FD93E81E CRC64;
MKHWGIRLRV LLVALAPVMA FGIAGGVWMV LHRLAELESS LIERGRATAR QVAATADYGI
FSGNTDALVS LIEAARREPD VSGIMVSSRD GDLAVSGGVL SPEAYLPGRR AAGLALVELD
HALMFVEPIV RSAVLDESDV FDGLGEPVTD RQPIGWVLVE VSRARVEAMK VDFILTSAGV
IAAALMLASV FAFRISRTVT GPVREVSQAV RRIGDGDLSV RLPVSGGGSL RVLAEGVNGM
AERLLRARDE LEARIADATR QLRSRTDEAE RANHAKSRFL AAASHDLRQP MHALGLFVAE
LAERLRGSEH RTLIRQIEES VGAMEDLLDA LLDMSKLDAG GVTVRRSHFP LQPMLSRIVD
DFAADALQRG LRLKLRATPL WVESDPLLLE RIMINLLSNA VRYTQRGGVL VCVRRRGQDA
VIEVRDSGPG IPAEAHDMIF EEFYQLQNPA RARGQGLGLG LAIVRRLSGL LGHDVAIRSR
AQHGSIFSVS VPCVAPPVGD VAEMEPAALP ASLSLFVIVI DDDPGSRNSV AGLLQSWGCD
VLCAPNLSEA RDAIRLRERS PALILCDFRL AAVASGIDVL DALLAEQGGE IAGALVTGDT
DPQVRRLAAA RGYPVLHKPV RPARLRALVQ QAVARQQNPV S
//
