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A-factor receptor protein (A-factor-binding protein)

 AFRP_STRGR              Reviewed;         276 AA.
Q9ZN78; Q54189;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-NOV-2018, entry version 83.
RecName: Full=A-factor receptor protein;
AltName: Full=A-factor-binding protein;
Name=arpA;
Streptomyces griseus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1911 {ECO:0000312|EMBL:BAA36282.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-21; 44-53 AND
148-167, SUBUNIT, INTERACTION WITH A-FACTOR, AND VARIANTS.
STRAIN=IFO 13350 / CBS 651.72;
PubMed=7592371; DOI=10.1128/jb.177.21.6083-6092.1995;
Onaka H., Ando N., Nihira T., Yamada Y., Beppu T., Horinouchi S.;
"Cloning and characterization of the A-factor receptor gene from
Streptomyces griseus.";
J. Bacteriol. 177:6083-6092(1995).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], DNA-BINDING, INTERACTION WITH
A-FACTOR, AND MUTAGENESIS OF VAL-41; TRP-119; GLU-135; PRO-138;
LYS-147; ILE-149; GLY-155; SER-160; ASP-163; ASP-168 AND PRO-187.
STRAIN=JA 5142;
PubMed=9813285; DOI=10.1016/S0378-1119(98)00487-9;
Sugiyama M., Onaka H., Nakagawa T., Horinouchi S.;
"Site-directed mutagenesis of the A-factor receptor protein: Val-41
important for DNA-binding and Trp-119 important for ligand-binding.";
Gene 222:133-144(1998).
[3] {ECO:0000305}
SUBCELLULAR LOCATION, AND INTERACTION WITH A-FACTOR.
PubMed=2502536; DOI=10.1128/jb.171.8.4298-4302.1989;
Miyake K., Horinouchi S., Yoshida M., Chiba N., Mori K., Nogawa N.,
Morikawa N., Beppu T.;
"Detection and properties of A-factor-binding protein from
Streptomyces griseus.";
J. Bacteriol. 171:4298-4302(1989).
[4] {ECO:0000305}
INTERACTION WITH A-FACTOR.
PubMed=2111804; DOI=10.1128/jb.172.6.3003-3008.1990;
Miyake K., Kuzuyama T., Horinouchi S., Beppu T.;
"The A-factor-binding protein of Streptomyces griseus negatively
controls streptomycin production and sporulation.";
J. Bacteriol. 172:3003-3008(1990).
[5] {ECO:0000305}
DNA-BINDING, AND INTERACTION WITH A-FACTOR.
PubMed=9220006; DOI=10.1046/j.1365-2958.1997.4081772.x;
Onaka H., Horinouchi S.;
"DNA-binding activity of the A-factor receptor protein and its
recognition DNA sequences.";
Mol. Microbiol. 24:991-1000(1997).
[6] {ECO:0000305}
FUNCTION.
PubMed=10540289; DOI=10.1046/j.1365-2958.1999.01579.x;
Ohnishi Y., Kameyama S., Onaka H., Horinouchi S.;
"The A-factor regulatory cascade leading to streptomycin biosynthesis
in Streptomyces griseus: identification of a target gene of the A-
factor receptor.";
Mol. Microbiol. 34:102-111(1999).
[7] {ECO:0000305}
MUTANT HO1.
PubMed=9098075; DOI=10.1128/jb.179.8.2748-2752.1997;
Onaka H., Sugiyama M., Horinouchi S.;
"A mutation at proline-115 in the A-factor receptor protein of
Streptomyces griseus abolishes DNA-binding ability but not ligand-
binding ability.";
J. Bacteriol. 179:2748-2752(1997).
-!- FUNCTION: Represses adpA expression by binding to the promoter
region in the absence of A-factor, causing repression of
streptomycin production and of sporulation.
{ECO:0000269|PubMed:10540289, ECO:0000303|PubMed:2111804}.
-!- SUBUNIT: Homodimer or multimer. Binds to both DNA and A-factor as
a homodimer. {ECO:0000269|PubMed:7592371}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2502536}.
-!- DOMAIN: Binds DNA through its N-terminal H-T-H motif and binds A-
factor via its C-terminal region. {ECO:0000269|PubMed:9813285}.
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EMBL; D49782; BAA08617.1; -; Genomic_DNA.
EMBL; AB021882; BAA36282.1; -; Genomic_DNA.
ProteinModelPortal; Q9ZN78; -.
SMR; Q9ZN78; -.
PRIDE; Q9ZN78; -.
eggNOG; ENOG41064MX; Bacteria.
eggNOG; ENOG41127CX; LUCA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; NAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
GO; GO:0019872; P:streptomycin biosynthetic process; NAS:UniProtKB.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001647; HTH_TetR.
InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
InterPro; IPR039419; TetR_trans_reg.
PANTHER; PTHR30328; PTHR30328; 1.
Pfam; PF00440; TetR_N; 1.
PRINTS; PR00455; HTHTETR.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF48498; SSF48498; 1.
PROSITE; PS50977; HTH_TETR_2; 1.
1: Evidence at protein level;
Cytoplasm; Direct protein sequencing; DNA-binding; Repressor;
Sporulation; Transcription; Transcription regulation.
CHAIN 1 276 A-factor receptor protein.
/FTId=PRO_0000070576.
DOMAIN 8 68 HTH tetR-type. {ECO:0000255|PROSITE-
ProRule:PRU00335}.
DNA_BIND 31 50 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00335}.
VARIANT 115 115 P -> S (in mutant HO1; lacks DNA-binding
activity).
VARIANT 171 171 G -> E (in strain: IFO 13350).
VARIANT 229 235 AATDSGS -> PTSEGGT (in strain: IFO
13350).
VARIANT 255 256 GA -> VT (in strain: IFO 13350).
VARIANT 274 274 V -> I (in strain: IFO 13350).
MUTAGEN 41 41 V->A: Loss of DNA-binding activity.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 119 119 W->A: Loss of A-factor-binding activity.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 135 135 E->A: Loss of both DNA-binding and A-
Factor-binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 138 138 P->A: No loss of DNA-binding or A-factor-
binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 147 147 K->A: No loss of DNA-binding or A-factor-
binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 149 149 I->A: Loss of both DNA-binding and A-
factor-binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 155 155 G->A: Loss of both DNA-binding and A-
factor-binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 160 160 S->A: No loss of DNA-binding or A-factor-
binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 163 163 D->A: No loss of DNA-binding or A-factor-
binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 168 168 D->A: Loss of both DNA-binding and A-
factor-binding activities.
{ECO:0000269|PubMed:9813285}.
MUTAGEN 187 187 P->A: No loss of DNA-binding or A-factor-
binding activities.
{ECO:0000269|PubMed:9813285}.
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


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