ID A0A2N0WVK3_9GAMM Unreviewed; 157 AA.
AC A0A2N0WVK3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN ORFNames=CW745_16345 {ECO:0000313|EMBL:PKF60185.1};
OS Psychromonas sp. psych-6C06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=2058089 {ECO:0000313|EMBL:PKF60185.1, ECO:0000313|Proteomes:UP000233619};
RN [1] {ECO:0000313|EMBL:PKF60185.1, ECO:0000313|Proteomes:UP000233619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psych-6C06 {ECO:0000313|Proteomes:UP000233619};
RX PubMed=27311813; DOI=.1038/ncomms11965;
RA Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT "Microbial interactions lead to rapid micro-scale successions on model
RT marine particles.";
RL Nat. Commun. 7:11965-11965(2016).
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:PKF60185.1}.
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DR EMBL; PIZM01000021; PKF60185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0WVK3; -.
DR OrthoDB; 9809748at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000233619; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233619};
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..157
FT /note="L,D-transpeptidase catalytic domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014916398"
FT DOMAIN 22..155
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 157 AA; 18023 MW; B664FD692E96AD79 CRC64;
MRYIFLIYML LSSSVFAGVD LVKVDKSDNK MYLMTDGKVL KEYYVAFGKT PKGHKEQEGD
QKTPEGTYTL DYKKEDSSFY RAMHISYPNA QDVKNAESKG VSAGGFIMVH GQRNWLGWFS
SITQKYNWTN GCIALTNPEM DEFMDLVETG TKIHIQW
//
