ID   IPSA_CORGL              Reviewed;         358 AA.
AC   Q8NMF0;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=HTH-type transcriptional regulator IpsA {ECO:0000305};
GN   Name=ipsA {ECO:0000303|PubMed:24377418};
GN   OrderedLocusNames=Cgl2627 {ECO:0000312|EMBL:BAC00021.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, SUBUNIT, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=24377418; DOI=10.1186/1741-7007-11-122;
RA   Baumgart M., Luder K., Grover S., Gaetgens C., Besra G.S., Frunzke J.;
RT   "IpsA, a novel LacI-type regulator, is required for inositol-derived lipid
RT   formation in Corynebacteria and Mycobacteria.";
RL   BMC Biol. 11:122-122(2013).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 2-356.
RA   Palani K., Burley S.K., Swaminathan S.;
RT   "Crystal structure of a transcriptional regulator, Lacl family protein from
RT   Corynebacterium glutamicum.";
RL   Submitted (APR-2009) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in the regulation of cell wall biogenesis.
CC       Inositol-dependent transcriptional activator of ino1, which encodes
CC       inositol phosphate synthase. Also regulates other target genes, which
CC       are most likely involved in the synthesis of inositol-derived cell wall
CC       components and mycothiol. Acts by binding to a conserved palindromic
CC       motif within the promoter regions. {ECO:0000269|PubMed:24377418}.
CC   -!- ACTIVITY REGULATION: Myo-inositol causes the dissociation of the IpsA-
CC       DNA complex in vitro. {ECO:0000269|PubMed:24377418}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24377418}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant shows growth defect and altered
CC       morphology. Mycothiol biosynthesis and phosphatidylinositol-based
CC       glycolipid synthesis are abolished. {ECO:0000269|PubMed:24377418}.
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DR   EMBL; BA000036; BAC00021.1; -; Genomic_DNA.
DR   RefSeq; NP_601828.1; NC_003450.3.
DR   PDB; 3H5T; X-ray; 2.53 A; A=2-356.
DR   PDBsum; 3H5T; -.
DR   AlphaFoldDB; Q8NMF0; -.
DR   SMR; Q8NMF0; -.
DR   STRING; 196627.cg2910; -.
DR   DNASU; 1020574; -.
DR   KEGG; cgl:Cgl2627; -.
DR   PATRIC; fig|196627.13.peg.2563; -.
DR   eggNOG; COG1609; Bacteria.
DR   HOGENOM; CLU_037628_6_1_11; -.
DR   OMA; IMQRYPS; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd01392; HTH_LacI; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR000843; HTH_LacI.
DR   InterPro; IPR046335; LacI/GalR-like_sensor.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF00356; LacI; 1.
DR   Pfam; PF13377; Peripla_BP_3; 1.
DR   SMART; SM00354; HTH_LACI; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS50932; HTH_LACI_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cell wall biogenesis/degradation; DNA-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..358
FT                   /note="HTH-type transcriptional regulator IpsA"
FT                   /id="PRO_0000442345"
FT   DOMAIN          8..63
FT                   /note="HTH lacI-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT   DNA_BIND        10..29
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ   SEQUENCE   358 AA;  38617 MW;  37B85603526D7E14 CRC64;
     MGRKQQYGTL ASIAAKLGIS RTTVSNAYNR PEQLSAELRQ RILDTAEDMG YLGPDPVARS
     LRTRRAGAIG VLLTEDLTYA FEDMASVDFL AGVAQAAGDT QLTLIPASPA SSVDHVSAQQ
     LVNNAAVDGV VIYSVAKGDP HIDAIRARGL PAVIADQPAR EEGMPFIAPN NRKAIAPAAQ
     ALIDAGHRKI GILSIRLDRA NNDGEVTRER LENAQYQVQR DRVRGAMEVF IEAGIDPGTV
     PIMECWINNR QHNFEVAKEL LETHPDLTAV LCTVDALAFG VLEYLKSVGK SAPADLSLTG
     FDGTHMALAR DLTTVIQPNK LKGFKAGETL LKMIDKEYVE PEVELETSFH PGSTVAPI