ID A0A419TD45_9FIRM Unreviewed; 477 AA.
AC A0A419TD45;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN ORFNames=BET01_00500 {ECO:0000313|EMBL:RKD35375.1};
OS Lacrimispora algidixylanolytica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD35375.1, ECO:0000313|Proteomes:UP000284277};
RN [1] {ECO:0000313|EMBL:RKD35375.1, ECO:0000313|Proteomes:UP000284277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPL73 {ECO:0000313|EMBL:RKD35375.1,
RC ECO:0000313|Proteomes:UP000284277};
RA Poppleton D.I., Gribaldo S.;
RT "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:RKD35375.1}.
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DR EMBL; MCIA01000001; RKD35375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419TD45; -.
DR OrthoDB; 177750at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000284277; 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; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF34; L,D-TRANSPEPTIDASE YCIB-RELATED; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51170; CW; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000284277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..477
FT /note="L,D-transpeptidase catalytic domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019024755"
FT REPEAT 288..307
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 323..444
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 30..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 52644 MW; B578AA4E74415B2B CRC64;
MRKLTYGLAA FCLTAVLVSG HTTYAWADEE RGPGLRNGVP ISQNDRQTET KDQGSKVTEE
AETALANAGI GIGAEAEGNG EDGVENEAAK AAQEALKANF PRLQSTVMTG DSNWSQPFVN
DAWITNNGEG FHGMSTFLTN IVGNVLYRTY TSSTGWSPWV LNGQQTTNYP NDVNIEAVQM
RFSGYVNNQF DVYYTAKLDD GSTMGWAKNG TTTGTMGTGH YITGFRMAFY TKNSAFPYST
EKPLISAVPD GITQVEGGLR YTNGDGSAFT GWAWSGNERY YFVDSNPVTG WQYIDGFKYY
FDETGRMLTD LEPVMGAKGP FLISINKQMN TMTVFAKDGN NGFIIPVKSF LTSTGPDTPL
GTYQTPEKYR WRDMNHGIYT QYATRIWKGF LIHSILYSRP NGMTLDSSTY NYLSIAESAG
CIRLLSGDAK WVYDHCALGT TVTIYNSVIP GPYERPAIEQ IIPDSQNWDP TDPNIAH
//
