ID A0A1T4MCH4_9BACT Unreviewed; 532 AA.
AC A0A1T4MCH4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:SJZ64567.1};
GN ORFNames=SAMN04488132_103310 {ECO:0000313|EMBL:SJZ64567.1};
OS Sediminibacterium ginsengisoli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Sediminibacterium.
OX NCBI_TaxID=413434 {ECO:0000313|EMBL:SJZ64567.1, ECO:0000313|Proteomes:UP000190888};
RN [1] {ECO:0000313|EMBL:SJZ64567.1, ECO:0000313|Proteomes:UP000190888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22335 {ECO:0000313|EMBL:SJZ64567.1,
RC ECO:0000313|Proteomes:UP000190888};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FUWH01000003; SJZ64567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4MCH4; -.
DR STRING; 413434.SAMN04488132_103310; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000190888; Unassembled WGS sequence.
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; IPR036365; PGBD-like_sf.
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.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000190888};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 68..203
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 316..465
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 532 AA; 59944 MW; 90EE72BB3ABE2E67 CRC64;
MRNFLLTSLV ALGFFTACNN EIKKEQQVSE RDLSITRVNA YNDLFLDTAA VNTFITKEQM
EPALANRFRS FYNRRNFQFA WLASDGLTEQ ARSFWNAVNY KQDSALEDKK LKAEMKDLWS
SSTQASASDK DNIRTELLLT KYFMNYMLTN YEQGTVKKKD LESLVPRKKE PVIVLADSFV
SKKAVNNEYE AANSSYKLLK DQLALYVGIA KKGGWQLFSV PAGKKFKKNG SDPLIPVIKK
HLALTGDMAA GDTTAVFNEP LEAGIKSYQA RMGYKPDGVI SPAIIKEMNV PVNKRIQQLV
INLDRMRWLP DGDNGKLIVT NIPEFKVHVY DGSRQEFEMP VVVGKDGHNT VIFTGTLSQV
VFSPYWNVPP SIVKNEILPK MNSDKSYLDQ EDMEVVSESG GLPVIRQRPG PKNSLGKVKF
LFPNDFNIYF HDTPAKSLFS QDQRAFSHGC IRLSDPVKMA NYLLKDDAGW DAAKINAAMN
AGKEKTVELK TKIPVLITYY TAWVDAAGKL NFRDDIYGHD AAVAHKMFTN PL
//
