AFSQ2_STRCO
ID AFSQ2_STRCO Reviewed; 535 AA.
AC Q04943;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Signal transduction histidine-protein kinase AfsQ2;
DE EC=2.7.13.3;
GN Name=afsQ2; OrderedLocusNames=SCO4906; ORFNames=2SCK8.32c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=1339426; DOI=10.1128/jb.174.23.7585-7594.1992;
RA Ishizuka H., Horinouchi S., Kieser H.M., Hopwood D.A., Beppu T.;
RT "A putative two-component regulatory system involved in secondary
RT metabolism in Streptomyces spp.";
RL J. Bacteriol. 174:7585-7594(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Forms part of a two-component regulatory system AfsQ1/AfsQ2
CC involved in secondary metabolism. May activate AfsQ1 by
CC phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D10654; BAA01503.1; -; Genomic_DNA.
DR EMBL; AL939121; CAC33071.1; -; Genomic_DNA.
DR PIR; B45270; B45270.
DR RefSeq; NP_629059.1; NC_003888.3.
DR RefSeq; WP_003974067.1; NZ_VNID01000016.1.
DR AlphaFoldDB; Q04943; -.
DR SMR; Q04943; -.
DR STRING; 100226.SCO4906; -.
DR GeneID; 1100347; -.
DR KEGG; sco:SCO4906; -.
DR PATRIC; fig|100226.15.peg.4985; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_18_11; -.
DR InParanoid; Q04943; -.
DR OMA; RRFVADM; -.
DR PhylomeDB; Q04943; -.
DR BRENDA; 2.7.13.3; 5998.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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 Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..535
FT /note="Signal transduction histidine-protein kinase AfsQ2"
FT /id="PRO_0000074683"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 224..276
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 291..510
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 493..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 294
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 535 AA; 57425 MW; D2D02CD5568AF73C CRC64;
MTREHQGGTR GLAAARKGFW SGLRFTSLRL RLVLVFGLVA LTAAVSASGI AYWLNREAVL
TRTQDAVLRD FEQEMQNRAG ALPEHPTQDE VQHTAGQMAN SSQRFSVLLV AENADGTAVY
GSSGGLGGVA LSDVPESLRT AVNKEQKLTS ANKHPYHLYW QRITDDGTPY LVAGTKVIGG
GPTGYMLKSL EPEAKDLNSL AWSLGIATAL ALLGSALLAQ ALATTVLKPV HRLGVAARRL
GEGKLDTRLR VSGTDELADL SRTFNSAAEN LEKRVADMAG REQASRRFVA DMSHELRTPL
TALTAVTEVL EEELEYAGEG EGEGGSFDPM VEPAVRLVVS ETRRLNDLVE NLMEVTRFDA
GTARLVLDDV DVADQITACI DARAWLDAVD LDAERGVHAR LDPRRLDVIL ANLIGNALKH
GGSPVRVSVA RADHEIVIRV RDNGPGIPED VLPHVFDRFY KASASRPRSE GSGLGLSIAL
ENAHIHGGEI TAENAPEGGA VFTLRLPQDP SPPADEDGGP DEETEDRGKD AKGQV
