LPPS_CORGL
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 03-AUG-2022, entry version 105.
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; 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 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 OMA; GDRRSHM; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000582; 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; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; -; 1.
DR InterPro; IPR041280; Big_10.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR Pfam; PF17964; Big_10; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; SSF141523; 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 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 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
