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Database: UniProt
Entry: S5YEX2_PARAH
LinkDB: S5YEX2_PARAH
Original site: S5YEX2_PARAH 
ID   S5YEX2_PARAH            Unreviewed;       179 AA.
AC   S5YEX2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN   ORFNames=JCM7686_2982 {ECO:0000313|EMBL:AGT10018.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT10018.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT10018.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT10018.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
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DR   EMBL; CP006650; AGT10018.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5YEX2; -.
DR   STRING; 1367847.JCM7686_2982; -.
DR   KEGG; pami:JCM7686_2982; -.
DR   PATRIC; fig|1367847.3.peg.2999; -.
DR   eggNOG; COG3034; Bacteria.
DR   HOGENOM; CLU_102842_0_1_5; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
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; 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   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..179
FT                   /note="L,D-transpeptidase catalytic domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004544692"
FT   DOMAIN          41..168
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   179 AA;  19490 MW;  25238D9A3DED9962 CRC64;
     MLNRLFRAVS ALFLVGLVAS CGGAKPEPTK FKSYDGPPVT QIVVKKGQRE MYLVSGQKVI
     KNYKIDLGSQ PVGAKQFEGD GKTPEGLYFI NRFNPNSLYH LSVGISYPNN DDRARAQMMG
     LRPGGDIMIH GLGPYGRAAN RPDWTAGCIA VNDQEIEEIY AMLARNGNGT TGVPVFILP
//
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