ID Q899Q5_CLOTE Unreviewed; 510 AA.
AC Q899Q5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN OrderedLocusNames=CTC_00115 {ECO:0000313|EMBL:AAO34767.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34767.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO34767.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; AE015927; AAO34767.1; -; Genomic_DNA.
DR AlphaFoldDB; Q899Q5; -.
DR STRING; 212717.CTC_00115; -.
DR KEGG; ctc:CTC_00115; -.
DR HOGENOM; CLU_533925_0_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001412; Chromosome.
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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..510
FT /note="L,D-transpeptidase catalytic domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004302455"
FT DOMAIN 391..509
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 292..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 58040 MW; 537B8125D7F6B522 CRC64;
MRGGQMTKSI NFKKVLYISL MLFTFLFNSN CKVNAETIKD VNNTNEINKV ENTSDKKEEK
FPLDKSTLLN SVEIKSNYNP IYNNRIVQFE VNSNYNNKLN YRALLHSKDK DSWQDVTSGY
TLNRNGNEVF QVNLFNVEVG DYELVIFAKT PASEGKYKAQ MGDYEIAYDD YKSKEFTCLK
NGEPDVSISF DNKTKMYEGA SKDISVKTNS YHGLVQYKVL MHSSNNGRWT DLSKGYTDEL
KSEDTYKINT GKLSAGNYKI AVRVKKAWDK GSKSDNLGDY DTSEVIEFSV LKKPTPPKKP
TQPSSKYPPA PKIEPLYVGN DSEITKIRVR KGPSLNTDIA GHIYGSTQEI KVLGRSGDFY
KVQATDYDSL NTINGYIKSN YVKKVIPNNT YSILVSLANQ KVYIYENNRL IKSFICSTGM
RGTPTIKGRF LIGGRGASFG QEHGYICYNF IRFNYDYLFH SVLHNLDGSI IQSEYNKLGT
QASHGCVRLK DEDIKWMYNN IPRNTLVVIQ
//
