ID   B0S3W7_FINM2            Unreviewed;       429 AA.
AC   B0S3W7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Putative carboxypeptidase {ECO:0000313|EMBL:BAG07741.1};
GN   OrderedLocusNames=FMG_0323 {ECO:0000313|EMBL:BAG07741.1};
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG07741.1, ECO:0000313|Proteomes:UP000001319};
RN   [1] {ECO:0000313|EMBL:BAG07741.1, ECO:0000313|Proteomes:UP000001319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC   {ECO:0000313|Proteomes:UP000001319};
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(2008).
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DR   EMBL; AP008971; BAG07741.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0S3W7; -.
DR   STRING; 334413.FMG_0323; -.
DR   KEGG; fma:FMG_0323; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   Proteomes; UP000001319; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF166; AMIDOHYDROLASE YHAA-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:BAG07741.1};
KW   Hydrolase {ECO:0000313|EMBL:BAG07741.1};
KW   Protease {ECO:0000313|EMBL:BAG07741.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001319}.
FT   DOMAIN          223..322
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   429 AA;  47803 MW;  89DFE2C7AAFD9652 CRC64;
     MLGFFTYFVF KIYILKMDNF SSKKGIYTTM KGELLMNYEK LFSLIDSKKD DMFNDRRWLH
     EHPELSYEEK ETSEYIYKHY ENNKNVKVEK NIGGYGVKVT IDSGKPGKTV ALRADFDALP
     ITEDTGLDYA SKNKGVMHAC GHDAHTAYMM TLADCLVEMK DDFSGKIVII HQPAEEMPPG
     GSSFMIKDGV LDGVDNIFGC HVMSQLDFGK VYYHKGPTQQ ARAKFVATVK GTGGHGAAPH
     EANDAIVIAS NLVMSLQTIV SRRLNPMTPG VVTIGSFDGK GQFNIIKDSV TLEGDVRCMS
     DDARVLIEKE VRNICEGLAK AYSCEIELDY KNDYPVLMND DEMTQLVVDA VKEAKIPEVV
     GVEDCGPQAQ SEDFSYYSQK IPASFFYIGA KPDGKAYPHH HPKFTINEDS MIIAAKAMGA
     VALKYLNEK
//