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Database: UniProt
Entry: A0A086Y423_9RHOB
LinkDB: A0A086Y423_9RHOB
Original site: A0A086Y423_9RHOB 
ID   A0A086Y423_9RHOB        Unreviewed;       169 AA.
AC   A0A086Y423;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN   ORFNames=CG50_12595 {ECO:0000313|EMBL:KFI29023.1};
OS   Paenirhodobacter enshiensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paenirhodobacter.
OX   NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI29023.1, ECO:0000313|Proteomes:UP000028824};
RN   [1] {ECO:0000313|EMBL:KFI29023.1, ECO:0000313|Proteomes:UP000028824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW2-9 {ECO:0000313|EMBL:KFI29023.1,
RC   ECO:0000313|Proteomes:UP000028824};
RA   Wang D., Wang G.;
RT   "Genome of Paenirhodobacter enshiensis DW2-9.";
RL   Submitted (MAR-2014) 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:KFI29023.1}.
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DR   EMBL; JFZB01000005; KFI29023.1; -; Genomic_DNA.
DR   RefSeq; WP_036635587.1; NZ_JFZB01000005.1.
DR   AlphaFoldDB; A0A086Y423; -.
DR   STRING; 1105367.CG50_12595; -.
DR   eggNOG; COG3034; Bacteria.
DR   OrthoDB; 9809748at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000028824; 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; 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:UP000028824};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..169
FT                   /note="L,D-transpeptidase catalytic domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001817403"
FT   DOMAIN          39..167
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   169 AA;  18599 MW;  5C081D6D6A7358C4 CRC64;
     MQRRTLILGL TSLTALAACG GDSSPKLLWP YVGPPITQVQ VYKKKRVMYL FSNDKIVRTY
     DIALGGNPIG KKRFEGDGKT PEGLYYINRR NPNSSYHLSL GLSYPNPTDI AYAQENGRRP
     GGDIFIHGRA GKDKGRGSDW TAGCVAVTDT EIEDIYAMVA VGTPVWIYP
//
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