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Database: UniProt
Entry: A0A1M6K7Z8_9FIRM
LinkDB: A0A1M6K7Z8_9FIRM
Original site: A0A1M6K7Z8_9FIRM 
ID   A0A1M6K7Z8_9FIRM        Unreviewed;       416 AA.
AC   A0A1M6K7Z8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:SHJ55079.1};
GN   ORFNames=SAMN02745136_00355 {ECO:0000313|EMBL:SHJ55079.1};
OS   Anaerocolumna jejuensis DSM 15929.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHJ55079.1, ECO:0000313|Proteomes:UP000184386};
RN   [1] {ECO:0000313|EMBL:SHJ55079.1, ECO:0000313|Proteomes:UP000184386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15929 {ECO:0000313|EMBL:SHJ55079.1,
RC   ECO:0000313|Proteomes:UP000184386};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; FRAC01000006; SHJ55079.1; -; Genomic_DNA.
DR   RefSeq; WP_073272340.1; NZ_FRAC01000006.1.
DR   AlphaFoldDB; A0A1M6K7Z8; -.
DR   STRING; 1121322.SAMN02745136_00355; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000184386; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184386}.
FT   DOMAIN          13..157
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..338
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   416 AA;  46953 MW;  AF957F9C504AA11A CRC64;
     MVNTRKLSNG ITVVFEPMPY LRSAALGIWV KVGSSNENAK NNGISHIIEH MLFKGTKTRT
     AKQIADEMAR IGGDINAYTS KECTSFYAVT LDEHLPIAIG ILGDMFNNSL FEEKSFQKEK
     GVIIEEIDMY DDSPEDLVHE MLQMKVWDKH PLGFQISGSK ETVRNTTRDE VLDYMTKHYV
     SDNMVISVAG NFKENEIMEL LEENFGKVPS GEKIEAAVAP SYVPTIYVKE KDVEQLHLNI
     AYESIISDGE EKYILTVLNS VFGGSINSRL FQEIRENLGL TYTIYSYGSS YSRAGLFHIY
     GAMNPSQLRP VVDNIFQIIE DIKENGITEE ELSMCKEQIK TELIMGDETA KNRMNSNGKA
     MLFRGYIIPL EEIIEKVNSV TKEEVKQFAL KYLNKEKVSI SLVGNLEGVD REGLLL
//
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