ID A0A1H9CM99_9FIRM Unreviewed; 450 AA.
AC A0A1H9CM99;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA (Peptidoglycan recycling) {ECO:0000313|EMBL:SEQ01803.1};
GN ORFNames=SAMN02910289_01103 {ECO:0000313|EMBL:SEQ01803.1};
OS Lachnospiraceae bacterium RM5.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1200721 {ECO:0000313|EMBL:SEQ01803.1, ECO:0000313|Proteomes:UP000199252};
RN [1] {ECO:0000313|EMBL:SEQ01803.1, ECO:0000313|Proteomes:UP000199252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM5 {ECO:0000313|EMBL:SEQ01803.1,
RC ECO:0000313|Proteomes:UP000199252};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; FOFK01000004; SEQ01803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9CM99; -.
DR STRING; 1200721.SAMN02910289_01103; -.
DR Proteomes; UP000199252; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:SEQ01803.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:SEQ01803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199252}.
FT DOMAIN 285..450
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 450 AA; 51482 MW; 33BA0ED5C9E05CE0 CRC64;
MLYGISNCSN GRNINNKSEI DSLKEVLNKN GIDTVFARNI YLSDDFSFAI GKERGKDLME
LYKNPDIEGI FDISGGDIAN EVLDYLDYDY IRNSKKTFFG YSDLTTVINA IYKVTGKVSV
LYQVRNVIKE NGKEQMENLK NFLFENGVLL TDIDYTFLAG NYMSGIVVGG NIRCFLKLAG
TKYFPDMKNK ILFLEALNGN ETILRTYFAQ LSQMGVFDEI SGILLGNFTE FERDNKNKTV
YDLLKQYINK KIPVAKTNEV GHSSDSKALR IGAFNRFCNI STDRLLLKPL SPRYVDSTYE
YASDTDNTKY MFFLPVESKE ESLRYLVRMN KEWMAEKNTD FEFVILKDNI HVGGISLTYS
EDRKTLELGW ILNKKYQGNK FAYEAAVSLL EFAKNVLGIT HFIAHCDADN VASYSLMEKL
GMKKISKTSG RMNRNAVKES YEYTYELSLK
//
