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Database: UniProt
Entry: A0QP10_MYCS2
LinkDB: A0QP10_MYCS2
Original site: A0QP10_MYCS2 
ID   A0QP10_MYCS2            Unreviewed;       346 AA.
AC   A0QP10;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Lipoprotein Lpps {ECO:0000313|EMBL:ABK76034.1};
GN   OrderedLocusNames=MSMEG_0233 {ECO:0000313|EMBL:ABK76034.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK76034.1, ECO:0000313|Proteomes:UP000000757};
RN   [1] {ECO:0000313|EMBL:ABK76034.1, ECO:0000313|Proteomes:UP000000757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; CP000480; ABK76034.1; -; Genomic_DNA.
DR   RefSeq; WP_011726764.1; NZ_SIJM01000047.1.
DR   RefSeq; YP_884648.1; NC_008596.1.
DR   AlphaFoldDB; A0QP10; -.
DR   SMR; A0QP10; -.
DR   STRING; 246196.MSMEG_0233; -.
DR   PaxDb; 246196-MSMEI_0226; -.
DR   GeneID; 66738421; -.
DR   KEGG; msm:MSMEG_0233; -.
DR   PATRIC; fig|246196.19.peg.229; -.
DR   eggNOG; COG1376; Bacteria.
DR   OrthoDB; 5242354at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000757; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13431; LDT_IgD_like_1; 1.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.60.40.3710; -; 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.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Lipoprotein {ECO:0000313|EMBL:ABK76034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..346
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002628933"
FT   DOMAIN          116..187
FT                   /note="Bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF17964"
FT   DOMAIN          202..326
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          28..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..65
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   346 AA;  37234 MW;  C04318B2C81B5D3E CRC64;
     MPKSAKRRLI TAFMAAGLVG GLVMSPSASA DPEVPAPPVP VEPAAPPAPP NPFAFPPPAA
     PAAVGPADPA TPGATATDPD AQVVTNYGAP AVPIEGVPEG QNPEPFTGQP PFLPPSFNPV
     NGSMVGVAKP IYINFQRPIA NKQMAQDAIR ITSNPPVPGR FYWVTDTQLR WRPQDFWPSN
     TVVNIDAAGT KSSFRVGDYL VATVDDSTHQ MEIRRNGKLE KTFPVSMGKN DGKHETKNGT
     YYVLEKFEDI VMDSSTYGVP VDSAEGYKLK VKDAVRIDNS GIFVHSAPWS VGDQGKRNVS
     HGCINLSPEN ARWFYEQFGS GDPVVIKNSK GGWYDQPDGA SDWQMF
//
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