AFRP_STRGR
ID AFRP_STRGR Reviewed; 276 AA.
AC Q9ZN78; Q54189;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=A-factor receptor protein;
DE AltName: Full=A-factor-binding protein;
GN Name=arpA;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911 {ECO:0000312|EMBL:BAA36282.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-21; 44-53 AND
RP 148-167, SUBUNIT, INTERACTION WITH A-FACTOR, AND VARIANTS.
RC STRAIN=IFO 13350 / CBS 651.72;
RX PubMed=7592371; DOI=10.1128/jb.177.21.6083-6092.1995;
RA Onaka H., Ando N., Nihira T., Yamada Y., Beppu T., Horinouchi S.;
RT "Cloning and characterization of the A-factor receptor gene from
RT Streptomyces griseus.";
RL J. Bacteriol. 177:6083-6092(1995).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DNA-BINDING, INTERACTION WITH A-FACTOR,
RP AND MUTAGENESIS OF VAL-41; TRP-119; GLU-135; PRO-138; LYS-147; ILE-149;
RP GLY-155; SER-160; ASP-163; ASP-168 AND PRO-187.
RC STRAIN=JA 5142;
RX PubMed=9813285; DOI=10.1016/s0378-1119(98)00487-9;
RA Sugiyama M., Onaka H., Nakagawa T., Horinouchi S.;
RT "Site-directed mutagenesis of the A-factor receptor protein: Val-41
RT important for DNA-binding and Trp-119 important for ligand-binding.";
RL Gene 222:133-144(1998).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND INTERACTION WITH A-FACTOR.
RX PubMed=2502536; DOI=10.1128/jb.171.8.4298-4302.1989;
RA Miyake K., Horinouchi S., Yoshida M., Chiba N., Mori K., Nogawa N.,
RA Morikawa N., Beppu T.;
RT "Detection and properties of A-factor-binding protein from Streptomyces
RT griseus.";
RL J. Bacteriol. 171:4298-4302(1989).
RN [4] {ECO:0000305}
RP INTERACTION WITH A-FACTOR.
RX PubMed=2111804; DOI=10.1128/jb.172.6.3003-3008.1990;
RA Miyake K., Kuzuyama T., Horinouchi S., Beppu T.;
RT "The A-factor-binding protein of Streptomyces griseus negatively controls
RT streptomycin production and sporulation.";
RL J. Bacteriol. 172:3003-3008(1990).
RN [5] {ECO:0000305}
RP DNA-BINDING, AND INTERACTION WITH A-FACTOR.
RX PubMed=9220006; DOI=10.1046/j.1365-2958.1997.4081772.x;
RA Onaka H., Horinouchi S.;
RT "DNA-binding activity of the A-factor receptor protein and its recognition
RT DNA sequences.";
RL Mol. Microbiol. 24:991-1000(1997).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=10540289; DOI=10.1046/j.1365-2958.1999.01579.x;
RA Ohnishi Y., Kameyama S., Onaka H., Horinouchi S.;
RT "The A-factor regulatory cascade leading to streptomycin biosynthesis in
RT Streptomyces griseus: identification of a target gene of the A-factor
RT receptor.";
RL Mol. Microbiol. 34:102-111(1999).
RN [7] {ECO:0000305}
RP MUTANT HO1.
RX PubMed=9098075; DOI=10.1128/jb.179.8.2748-2752.1997;
RA Onaka H., Sugiyama M., Horinouchi S.;
RT "A mutation at proline-115 in the A-factor receptor protein of Streptomyces
RT griseus abolishes DNA-binding ability but not ligand-binding ability.";
RL J. Bacteriol. 179:2748-2752(1997).
CC -!- FUNCTION: Represses adpA expression by binding to the promoter region
CC in the absence of A-factor, causing repression of streptomycin
CC production and of sporulation. {ECO:0000269|PubMed:10540289,
CC ECO:0000303|PubMed:2111804}.
CC -!- SUBUNIT: Homodimer or multimer. Binds to both DNA and A-factor as a
CC homodimer. {ECO:0000269|PubMed:7592371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2502536}.
CC -!- DOMAIN: Binds DNA through its N-terminal H-T-H motif and binds A-factor
CC via its C-terminal region. {ECO:0000269|PubMed:9813285}.
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DR EMBL; D49782; BAA08617.1; -; Genomic_DNA.
DR EMBL; AB021882; BAA36282.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZN78; -.
DR SMR; Q9ZN78; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0019872; P:streptomycin biosynthetic process; NAS:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Repressor; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..276
FT /note="A-factor receptor protein"
FT /id="PRO_0000070576"
FT DOMAIN 8..68
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 31..50
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT REGION 207..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 115
FT /note="P -> S (in mutant HO1; lacks DNA-binding activity)"
FT VARIANT 171
FT /note="G -> E (in strain: IFO 13350)"
FT VARIANT 229..235
FT /note="AATDSGS -> PTSEGGT (in strain: IFO 13350)"
FT VARIANT 255..256
FT /note="GA -> VT (in strain: IFO 13350)"
FT VARIANT 274
FT /note="V -> I (in strain: IFO 13350)"
FT MUTAGEN 41
FT /note="V->A: Loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 119
FT /note="W->A: Loss of A-factor-binding activity."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 135
FT /note="E->A: Loss of both DNA-binding and A-Factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 138
FT /note="P->A: No loss of DNA-binding or A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 147
FT /note="K->A: No loss of DNA-binding or A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 149
FT /note="I->A: Loss of both DNA-binding and A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 155
FT /note="G->A: Loss of both DNA-binding and A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 160
FT /note="S->A: No loss of DNA-binding or A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 163
FT /note="D->A: No loss of DNA-binding or A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 168
FT /note="D->A: Loss of both DNA-binding and A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
FT MUTAGEN 187
FT /note="P->A: No loss of DNA-binding or A-factor-binding
FT activities."
FT /evidence="ECO:0000269|PubMed:9813285"
SQ SEQUENCE 276 AA; 28950 MW; 6940BC3105D35CE0 CRC64;
MAKQARAVQT WRSIVDAAAS VFDDYGYERA AISEILRRAK VTKGALYFHF ASKEAIAQAI
MDEQTSTVEF EQEGSPLQSL VDGGQQFAFA LRHNSMARAG TRLSIEGVFL GGPHPWGDWI
DATARMLELG QERGEVFPQI DPMVSAKIIV ASFTGIQLVS EADSGRADLR GQVAEMWRHI
LPSIAHPGVI AHIKPEGRVD LAAQAREKAE REEQEARIAA EAKGAGSDAA TDSGSRSGGS
GLRGGGSGRG PRAGGAGDEG DEEPAGAGVA AGGVVA
