ID A0A257GQU9_9RHOB Unreviewed; 227 AA.
AC A0A257GQU9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN ORFNames=CFE33_01240 {ECO:0000313|EMBL:OYU40747.1};
OS Pseudorhodobacter sp. PARRP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2015560 {ECO:0000313|EMBL:OYU40747.1, ECO:0000313|Proteomes:UP000215760};
RN [1] {ECO:0000313|EMBL:OYU40747.1, ECO:0000313|Proteomes:UP000215760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PARRP1 {ECO:0000313|EMBL:OYU40747.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU40747.1}.
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DR EMBL; NKIU01000001; OYU40747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257GQU9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000215760; 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; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000215760};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..227
FT /note="L,D-transpeptidase catalytic domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012784722"
FT DOMAIN 77..214
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 227 AA; 24649 MW; 96987AEA63415ED9 CRC64;
MFTRRAFMAA ASAASLSACA AKPPEAAPPP PPPPMPARYG AIYTEPHPVP AIPDGIVDAR
LWRQEVENPF PFETTGTIIV DPDAAFLHLV TAPDRALRYG VSVGAAGYGW NGDAKVQFRR
KWPVWKAPDE MIARRPEFAP YSVANGGMPG GPGNPLGARA LYLFQDGKDT LYRIHGACEP
KYLGKSVSSG CIRMLDQDVI DLHDRVQDGA KVVVLPSVRN HTFEVPY
//
