ID E7GHI1_CLOSY Unreviewed; 305 AA.
AC E7GHI1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:EGA95814.1};
GN ORFNames=HMPREF9474_00374 {ECO:0000313|EMBL:EGA95814.1};
OS [Clostridium] symbiosum WAL-14163.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA95814.1, ECO:0000313|Proteomes:UP000002970};
RN [1] {ECO:0000313|EMBL:EGA95814.1, ECO:0000313|Proteomes:UP000002970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA95814.1,
RC ECO:0000313|Proteomes:UP000002970};
RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA Molitoris D.R., Vaisanen M.L., Daigneault M., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium symbiosum strain WAL-14163.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:EGA95814.1}.
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DR EMBL; ADLQ01000011; EGA95814.1; -; Genomic_DNA.
DR RefSeq; WP_003497716.1; NZ_GL834305.1.
DR AlphaFoldDB; E7GHI1; -.
DR STRING; 1512.GCA_900049235_00416; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_1_1_9; -.
DR Proteomes; UP000002970; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 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; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
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; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EGA95814.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:EGA95814.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002970}.
FT DOMAIN 20..135
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 181..294
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 305 AA; 33810 MW; 6AF80E07D20B7573 CRC64;
MEPGENLYMG GGILRRGDRV GLSCCSNGLL EADKGSLELL KERLALIGLE AVESPFLYRG
VTAFSGTGTQ RAHALMDFYR DETVKAVFDV SGGDMANEVL TDLDFEMISA SDKIFFGYSD
LTTVINAIYT KTGKKSGLYQ LRNLTGPCWQ EQFSQFRETL MEGGSMLNNF SFHFLRGTRM
EGTVLGGNIR CLLKLAGTQY WPDFTGKLLF LECNGGEVPQ IVAYLNQLSQ LGVFCQISGI
LLGTFSRMEN RGLHPTVEEL LLRMIRPELP VAKTFQIGHG SDSRCLMIGD HIRIHQALQE
QKPPA
//
