ID A0A0Q4MY60_9GAMM Unreviewed; 251 AA.
AC A0A0Q4MY60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:KQN55721.1};
GN ORFNames=ASF13_09555 {ECO:0000313|EMBL:KQN55721.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN55721.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN55721.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN55721.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN55721.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN55721.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Global transcription factor that controls the expression of
CC over 100 target genes in response to anoxia. It facilitates the
CC adaptation to anaerobic growth conditions by regulating the expression
CC of gene products that are involved in anaerobic energy metabolism. When
CC the terminal electron acceptor, O(2), is no longer available, it
CC represses the synthesis of enzymes involved in aerobic respiration and
CC increases the synthesis of enzymes required for anaerobic respiration.
CC {ECO:0000256|ARBA:ARBA00037339}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KQN55721.1}.
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DR EMBL; LMLK01000022; KQN55721.1; -; Genomic_DNA.
DR RefSeq; WP_056238130.1; NZ_LMLK01000022.1.
DR AlphaFoldDB; A0A0Q4MY60; -.
DR STRING; 1736225.ASF13_09555; -.
DR Proteomes; UP000050856; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00092; HTH_CRP; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR PANTHER; PTHR24567:SF75; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00325; Crp; 1.
DR PRINTS; PR00034; HTHCRP.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00042; HTH_CRP_1; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000050856}.
FT DOMAIN 31..114
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 165..238
FT /note="HTH crp-type"
FT /evidence="ECO:0000259|PROSITE:PS51063"
SQ SEQUENCE 251 AA; 28082 MW; 6978FD606F64088F CRC64;
MIPEKRIISR RVQSGGCAIH CQDCSISQLC IPFTLNEHEL DQLDNIIERK KPIQKGQTLF
KAGDELKSIY AIRAGTIKSY TITEQGDEQI TGFHLAGDLV GFDAISANQH PSFAQALETA
MVCEIPFETL DDLSGKMPNL RQQIMRLMSG EIKGDQEMIL LLSKKNAEER LAAFIYGLSR
RFGQRGFSQR EFRLTMTRGD IGNYLGLTVE TISRLLGRFQ KNGMLAVKGK YITIENHEIL
SQLAGQSRAI G
//
