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Database: UniProt
Entry: Q8NMT9
LinkDB: Q8NMT9
Original site: Q8NMT9 
ID   LPPS_CORGL              Reviewed;         403 AA.
AC   Q8NMT9; Q6M2Z3;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Putative L,D-transpeptidase LppS;
DE            EC=2.3.2.-;
DE   AltName: Full=Putative lipoprotein LppS;
DE   Flags: Precursor;
GN   Name=lppS; OrderedLocusNames=Cgl2475, cg2720;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   GLYCOSYLATION.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=16734784; DOI=10.1111/j.1574-6968.2006.00269.x;
RA   Mahne M., Tauch A., Puhler A., Kalinowski J.;
RT   "The Corynebacterium glutamicum gene pmt encoding a glycosyltransferase
RT   related to eukaryotic protein-O-mannosyltransferases is essential for
RT   glycosylation of the resuscitation promoting factor (Rpf2) and other
RT   secreted proteins.";
RL   FEMS Microbiol. Lett. 259:226-233(2006).
CC   -!- FUNCTION: May play a role in cell wall biology. {ECO:0000305}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Secreted {ECO:0000269|PubMed:16734784}.
CC   -!- PTM: Glycosylated; by Pmt. {ECO:0000269|PubMed:16734784}.
CC   -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
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DR   EMBL; BA000036; BAB99868.1; -; Genomic_DNA.
DR   EMBL; BX927155; CAF21137.1; -; Genomic_DNA.
DR   RefSeq; NP_601675.1; NC_003450.3.
DR   RefSeq; WP_011015151.1; NC_006958.1.
DR   AlphaFoldDB; Q8NMT9; -.
DR   SMR; Q8NMT9; -.
DR   STRING; 196627.cg2720; -.
DR   KEGG; cgb:cg2720; -.
DR   KEGG; cgl:Cgl2475; -.
DR   PATRIC; fig|196627.13.peg.2407; -.
DR   eggNOG; COG1376; Bacteria.
DR   HOGENOM; CLU_039404_3_0_11; -.
DR   OrthoDB; 5242354at2; -.
DR   BioCyc; CORYNE:G18NG-12076-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000582; Chromosome.
DR   Proteomes; UP000001009; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd13432; LDT_IgD_like_2; 1.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.60.40.3710; -; 1.
DR   Gene3D; 2.60.40.3780; -; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR041280; Big_10.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF35; L,D-TRANSPEPTIDASE 2; 1.
DR   Pfam; PF17964; Big_10; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   PROSITE; PS52029; LD_TPASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Peptidoglycan synthesis; Reference proteome; Secreted; Signal;
KW   Transferase.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           29..403
FT                   /note="Putative L,D-transpeptidase LppS"
FT                   /id="PRO_0000421159"
FT   DOMAIN          243..369
FT                   /note="L,D-TPase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01373"
FT   REGION          35..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01373"
FT   ACT_SITE        345
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01373"
FT   LIPID           29
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           29
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   403 AA;  43401 MW;  27B96BBE2AB99D34 CRC64;
     MRVFRGRRGA VAGSFLAVLA IGSLALTGCT IERSDAQEQS SQQSTEVEAE EAQAPVISVD
     DGDEDVDPSE SVIVKSMGDG LSKVTMTNEE GYEVESELSD DGRSWTTAET LGYNRTYTIK
     ATDKNGETAT ASFSTATPAA TTNVALSPLA DSVVGVGQTI GFRFGSPVKD RKAAQDAITV
     TTSPKVEGGF YWLNNSELRW RPAEYWEPGT EVTVEADIYG KDLGGGVWGE TDNATNFTIG
     DKVEAVADDA TKTMSVYKNG ELLRTMPVSF GRDTSEWATP NGTYIIGDRN ESMIMDSTTF
     GLGYEEGGYR TPVKYATQMS YSGIYVHAAP WSVGAQGSYN TSHGCINVST ENAQWFQEAV
     KRGDIVTVKN TIGETLSGYD GLGDWNIPWS EWSKGNADQT SAW
//
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