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Database: UniProt
Entry: A0A3P3DHQ3_9RHOB
LinkDB: A0A3P3DHQ3_9RHOB
Original site: A0A3P3DHQ3_9RHOB 
ID   A0A3P3DHQ3_9RHOB        Unreviewed;       238 AA.
AC   A0A3P3DHQ3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=L,D-transpeptidase {ECO:0000313|EMBL:RRH73799.1};
GN   ORFNames=EG244_12045 {ECO:0000313|EMBL:RRH73799.1};
OS   Falsigemmobacter faecalis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Falsigemmobacter.
OX   NCBI_TaxID=2488730 {ECO:0000313|EMBL:RRH73799.1, ECO:0000313|Proteomes:UP000282125};
RN   [1] {ECO:0000313|EMBL:RRH73799.1, ECO:0000313|Proteomes:UP000282125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 102744-1 {ECO:0000313|EMBL:RRH73799.1,
RC   ECO:0000313|Proteomes:UP000282125};
RA   Li G., Jiang Y.;
RT   "Gemmobacter sp. nov., YIM 102744-1 draft genome.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RRH73799.1}.
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DR   EMBL; RRAZ01000016; RRH73799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P3DHQ3; -.
DR   OrthoDB; 9795305at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000282125; Unassembled WGS sequence.
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; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..238
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018116714"
FT   DOMAIN          82..217
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   238 AA;  26100 MW;  ACEBAFE79853A0F7 CRC64;
     MLRRPFLPGT APGLLFLVLA ACAAPQPPEP PPAPAHLTPE VLAHYGSRPD GEVELPAVPA
     RYLSPENLRQ EVNFITDERP GTVIVDPWTR HLYYVLPENR AVRYRVAVGD EGRAFSGQAT
     IPYSRSWPSW RPTENMIREF PDQYGPLRGG MDGGLMNPLG ARALYLHRGG KDTFYRIHGT
     SDVTSIGNAT SAGCIRMFHQ DVIELETLVK SGAKVVVLTE EQSDDLSARQ GSSPKLGS
//
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