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Database: UniProt
Entry: A0A2A8CY22_9BACT
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ID   A0A2A8CY22_9BACT        Unreviewed;       418 AA.
AC   A0A2A8CY22;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:PEN13612.1};
GN   ORFNames=CRI94_09905 {ECO:0000313|EMBL:PEN13612.1};
OS   Longibacter salinarum.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC   Longibacter.
OX   NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN13612.1, ECO:0000313|Proteomes:UP000220102};
RN   [1] {ECO:0000313|EMBL:PEN13612.1, ECO:0000313|Proteomes:UP000220102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN13612.1,
RC   ECO:0000313|Proteomes:UP000220102};
RA   Goh K.M., Shamsir M.S., Lim S.W.;
RT   "Draft genome of Longibacter Salinarum.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PEN13612.1}.
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DR   EMBL; PDEQ01000004; PEN13612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8CY22; -.
DR   OrthoDB; 9776731at2; -.
DR   Proteomes; UP000220102; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03886; M20_Acy1; 1.
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:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-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   Hydrolase {ECO:0000313|EMBL:PEN13612.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220102}.
FT   DOMAIN          203..299
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   418 AA;  44819 MW;  CEB8D3A6E90915A2 CRC64;
     MKQRIHSLAD EVFPDVVAWR RQIHQNPELA REEHQTASLV ADTLRRLDLD VRTGIYGTGV
     VGTLRGAHPG PTILLRADMD ALPIHEATGL NFASNHEGQM HACGHDAHTA SLLGAATILS
     RIRDEIHGQI RFCFQPSEEV IPGGAKFMIE EGVLESFGSA GDGASGDRSE DGVDYVFGQH
     VRPDLPVGTV GIRSGPFMAS ADEVHITVRG EGGHAAAPHE LSADATYVAS QIVVGLQSIV
     SRHAPPGVAS ILTIGRLIAD GATNVIPETA RLAGTFRAMD EEWRAEAHKL IERLIHRTAE
     AHGATAEVDL KVGYPALIND SEAAALVRDA SLEFTGADQT LDLNPWYAGE DFAYFLQKRP
     GAFFTLGVGN PERGITHGLH TPKFDIDEEA LRIGAGFMAY LAWTCGVEKP TTSDLAAS
//
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