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Database: UniProt
Entry: A0A0C2G7Q8_9ACTN
LinkDB: A0A0C2G7Q8_9ACTN
Original site: A0A0C2G7Q8_9ACTN 
ID   A0A0C2G7Q8_9ACTN        Unreviewed;       225 AA.
AC   A0A0C2G7Q8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA-binding response regulator MtrA {ECO:0000256|ARBA:ARBA00035142};
GN   ORFNames=LP52_08195 {ECO:0000313|EMBL:KIH99333.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH99333.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
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:KIH99333.1}.
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DR   EMBL; JROO01000013; KIH99333.1; -; Genomic_DNA.
DR   RefSeq; WP_040272122.1; NZ_JROO01000013.1.
DR   AlphaFoldDB; A0A0C2G7Q8; -.
DR   STRING; 183763.LP52_08195; -.
DR   OrthoDB; 116118at2; -.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd17626; REC_OmpR_MtrA-like; 1.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.690; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR047673; MtrA_REC.
DR   InterPro; IPR047671; MtrAB_MtrA.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; NF040689; MtrAB_MtrA; 1.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR   PANTHER; PTHR48111:SF79; TRANSCRIPTIONAL REGULATORY PROTEIN AFSQ1; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675}.
FT   DOMAIN          4..117
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          125..224
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        125..224
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   225 AA;  24896 MW;  80EC986C44E5A13F CRC64;
     MKGRVLVVDD DLALAEMLGI VLRGEGFEPS FVHDGDKALE AFRETKPDLV LLDLMLPGAD
     GIDVCRQIRA ESGVPIVMLT AKSDTVDIVL GLESGADDYI VKPFKPKELV ARVRVRLRRT
     EEPAPEVLQI GDITIDVAGH SVRRDGEPIS LTPLEFDLLV ALARKPRQVF TREVLLEQVW
     GYRHAADTRL VNVHVQRLRA KIEKDPEHPE VVVTVRGVGY KAGTA
//
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