ID A0A2K2TPU9_9CLOT Unreviewed; 486 AA.
AC A0A2K2TPU9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=L,D-transpeptidase {ECO:0000313|EMBL:PNV59958.1};
GN ORFNames=C0033_21050 {ECO:0000313|EMBL:PNV59958.1};
OS Clostridium sp. chh4-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2067550 {ECO:0000313|EMBL:PNV59958.1, ECO:0000313|Proteomes:UP000236356};
RN [1] {ECO:0000313|Proteomes:UP000236356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=chh4-2 {ECO:0000313|Proteomes:UP000236356};
RA Huang C.-H.;
RT "Clostridium sp. nov. strain chh-4-2., isolated from the gut of a healthy
RT Taiwan adult.";
RL Submitted (JAN-2018) 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}.
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:PNV59958.1}.
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DR EMBL; PKUU01000024; PNV59958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2TPU9; -.
DR OrthoDB; 177750at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000236356; 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:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000236356};
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..486
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014340405"
FT REPEAT 293..312
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 326..451
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 37..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 53289 MW; 08D63DE401460F13 CRC64;
MHKLFRSSAA LMMACAMFTM SSMTAFAEEG YGPGFNLPDK YESTEQTGDS AQTGSAENNT
TSGASENQTQ ETTAGQETGG QTADELAAEL ASAEAAEAAA RANLPQLQTT VLIPGSVWSQ
PFVNDQQIAL GDGLGFRSIS IFLTNTVGNV LYRTYSTQYG WTPWVMNGQY TTVYADETQM
EAIQLKLDGP VSNTFDIYYC SILSDGTTTG WTKNGEASGT MGTDKKIVGF RMALNGKDVE
WPHSTEHVLD SVHDDGVQYI DGQLRYINGD GTNFTGWGYV GSDRYYFVDS MPVTGWQYID
GYKLYFNEAG VLVKDLDPII GKQSTYQIKI NKEMNVTTVY AADGANGFII PVKSFLCSTG
DDTPLGTFKT PEKYRWRLMN SGVYAQYATR LAAGQSFLLH SIIYEKQNNM TLQPSTYNYL
GVARSAGCIR YLTQDAKWIF DNCPVGTTVT VYNAQDPGPY GRPVIPYTIP DTQTWDPTDV
TVTGVN
//
