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Database: UniProt
Entry: A0A1B7LHN5_9FIRM
LinkDB: A0A1B7LHN5_9FIRM
Original site: A0A1B7LHN5_9FIRM 
ID   A0A1B7LHN5_9FIRM        Unreviewed;       312 AA.
AC   A0A1B7LHN5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A6M21_04720 {ECO:0000313|EMBL:OAT85797.1};
OS   Desulfotomaculum copahuensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT85797.1, ECO:0000313|Proteomes:UP000078532};
RN   [1] {ECO:0000313|EMBL:OAT85797.1, ECO:0000313|Proteomes:UP000078532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMa1 {ECO:0000313|EMBL:OAT85797.1,
RC   ECO:0000313|Proteomes:UP000078532};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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}.
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:OAT85797.1}.
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DR   EMBL; LYVF01000047; OAT85797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7LHN5; -.
DR   STRING; 1838280.A6M21_04720; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000078532; 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   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
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; PF01471; PG_binding_1; 2.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078532};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..312
FT                   /note="ErfK/YbiS/YcfS/YnhG family protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008596940"
FT   DOMAIN          49..105
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          136..234
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   DOMAIN          255..298
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
SQ   SEQUENCE   312 AA;  33842 MW;  CD63E1DDA3F02906 CRC64;
     MVFYLFKILL TAATVFFCCS LPPLPAAAGP AGHRCDPVEP HVFTAPFHQG GDVASLQRCL
     AYLGYFHGAA SGYYDRATMA ALGNFQRQHH LSPSGLMDAP TWQVISRAML IRAQAEEKIP
     SPHHDLCLLI DTFNLTLTVF SRGEIIRQYP VAVGRPGEET PVGSWRVANK SDEHLPGMGP
     RWMGLNIPGG SYGIHGTDRP WSIGTYASAG CVRMHNAHVL ELFPWVTEGT PVLILGNPFG
     RFGEPYPVLQ PGSCGAAVQE VQRVLKRLGY YQKSPDGVFG PGTADAVNLL RIQNGLPAGR
     VVDGPVYRLL GI
//
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