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Database: UniProt
Entry: A0A074T9A9_9RHOB
LinkDB: A0A074T9A9_9RHOB
Original site: A0A074T9A9_9RHOB 
ID   A0A074T9A9_9RHOB        Unreviewed;       221 AA.
AC   A0A074T9A9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN   ORFNames=DL1_12085 {ECO:0000313|EMBL:KEP68381.1};
OS   Thioclava dalianensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP68381.1, ECO:0000313|Proteomes:UP000027725};
RN   [1] {ECO:0000313|EMBL:KEP68381.1, ECO:0000313|Proteomes:UP000027725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP68381.1,
RC   ECO:0000313|Proteomes:UP000027725};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
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:KEP68381.1}.
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DR   EMBL; JHEH01000034; KEP68381.1; -; Genomic_DNA.
DR   RefSeq; WP_026155629.1; NZ_JHEH01000034.1.
DR   AlphaFoldDB; A0A074T9A9; -.
DR   STRING; 1185766.SAMN05216224_11331; -.
DR   eggNOG; COG1376; Bacteria.
DR   OrthoDB; 9795305at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000027725; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027725};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..221
FT                   /note="L,D-transpeptidase catalytic domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001699570"
FT   DOMAIN          75..207
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   221 AA;  24422 MW;  52A168923A8E05B5 CRC64;
     MLTRRHFIQT TTALFSVTGP GMAFADTWPT EAQKAEWDAQ VTPQGYVAET SNPWGLHPRF
     LPQRVVAKAG LVPGDIHVDA VARYLYHIEE GGTAMRYGVA IARGNLYEPG VYTIKRKVRW
     PHWQPTQSMI NRDPELYADI ADGMEPGPEN ALGSRALYLY VGDRDTLLRI HGTPSPRSIG
     GRASSGCVRM VMAHINDLYP NVETGSTAYL YSAEDSVTAR S
//
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