ID   B9KD17_CAMLR            Unreviewed;       323 AA.
AC   B9KD17;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 2.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Peptidoglycan LD-carboxypeptidase {ECO:0000313|EMBL:ACM64456.2};
GN   Name=pgp2 {ECO:0000313|EMBL:ACM64456.2};
GN   OrderedLocusNames=Cla_1134 {ECO:0000313|EMBL:ACM64456.2};
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM64456.2, ECO:0000313|Proteomes:UP000007727};
RN   [1] {ECO:0000313|EMBL:ACM64456.2, ECO:0000313|Proteomes:UP000007727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060
RC   {ECO:0000313|Proteomes:UP000007727};
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; CP000932; ACM64456.2; -; Genomic_DNA.
DR   RefSeq; WP_012661840.1; NC_012039.1.
DR   AlphaFoldDB; B9KD17; -.
DR   STRING; 306263.Cla_1135; -.
DR   GeneID; 7410869; -.
DR   KEGG; cla:CLA_1134; -.
DR   PATRIC; fig|306263.5.peg.1119; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_7; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007727; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR36699:SF1; L,D-TRANSPEPTIDASE YAFK-RELATED; 1.
DR   PANTHER; PTHR36699; LD-TRANSPEPTIDASE; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ACM64456.2};
KW   Hydrolase {ECO:0000313|EMBL:ACM64456.2};
KW   Protease {ECO:0000313|EMBL:ACM64456.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          66..189
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   323 AA;  37551 MW;  3D0208E334E68E79 CRC64;
     MFKTILVLFS LVVFVNASDL AKIYLNQGID AVEKVLEQEL SKKDFWLDEI KDKNVSLGYY
     EENVAIVLTN KSDKIIRVYH YNDGKVEKKF IQKDVLTGLA GDKEIEGDLK TPIGFYELGK
     KFYPGDPYYG PFAFATTYPN VLDKTLGKTG GGIWIHGYPL DGTRLDTYKT RGCIAVQNDL
     LEDFNKLVAD RKSYAMTEEK NKVRANHEEV AILLANLFAW KDSWQKSDIS KYLSFYDQKI
     FKHNNKFSYE QFAKNKQRIF AKKEEKTIKF SDLSISPYPN DKNEKIFRIG FYEDYRSTNY
     KFKGEKVLYV KLVEDKMQIL AEQ
//