ID A0A1G5T5N6_9SPHN Unreviewed; 384 AA.
AC A0A1G5T5N6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:SDA16564.1};
GN ORFNames=SAMN03159340_00937 {ECO:0000313|EMBL:SDA16564.1};
OS Sphingomonas sp. NFR15.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1566282 {ECO:0000313|EMBL:SDA16564.1, ECO:0000313|Proteomes:UP000199327};
RN [1] {ECO:0000313|Proteomes:UP000199327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR15 {ECO:0000313|Proteomes:UP000199327};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMWX01000001; SDA16564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5T5N6; -.
DR STRING; 1566282.SAMN03159340_00937; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199327; 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; IPR045380; LD_TPept_scaffold_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR41533:SF2; BLR7131 PROTEIN; 1.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR Pfam; PF20142; Scaffold; 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:UP000199327};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..384
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011752243"
FT DOMAIN 24..141
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 171..312
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 384 AA; 41520 MW; B40AC1883D3CE69E CRC64;
MTRAVLLCCF LSLVSAAPAP DVVQPHWTRP QAARLVEWLD AAADDALEPV TAQARIVRAA
LDTNDQAALD AAATEAATRL LEAHRHGCCG AALRSGWHIA DTSDRTDAAT RVGQAVAADR
IDALFASARP SHPYYLALRA AYHAESDPAR RATLAANLDR WRWMPRALGT RYLLVNTAAF
EATLWEDGKM TGRWRVVAGK TASPTPVFAA TVTGVILNPW WEIPPSIARE GIAALLRTHP
AQAAAQGYVL QAGRYRQRPG ANNALGRMKL VMPNGYSVYL HDTPEQKLFA EDVRAYSHGC
VRVGDALGLV AALLSKQPGW TRGDVDAAVA TGRTRTVALA APVPIYIAYF TAEPDDKGDI
RYIADIYHRD TGAKLRGDQG QCAR
//
