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Database: UniProt
Entry: A0A1N6G5Z4_9LACT
LinkDB: A0A1N6G5Z4_9LACT
Original site: A0A1N6G5Z4_9LACT 
ID   A0A1N6G5Z4_9LACT        Unreviewed;       603 AA.
AC   A0A1N6G5Z4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:SIO02950.1};
GN   ORFNames=SAMN05878443_1043 {ECO:0000313|EMBL:SIO02950.1};
OS   Carnobacterium alterfunditum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=28230 {ECO:0000313|EMBL:SIO02950.1, ECO:0000313|Proteomes:UP000184758};
RN   [1] {ECO:0000313|EMBL:SIO02950.1, ECO:0000313|Proteomes:UP000184758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=313 {ECO:0000313|EMBL:SIO02950.1,
RC   ECO:0000313|Proteomes:UP000184758};
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|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; FSRN01000001; SIO02950.1; -; Genomic_DNA.
DR   RefSeq; WP_034547866.1; NZ_FSRN01000001.1.
DR   AlphaFoldDB; A0A1N6G5Z4; -.
DR   STRING; 28230.SAMN05878443_1043; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 9769691at2; -.
DR   Proteomes; UP000184758; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          115..179
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          345..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   603 AA;  68603 MW;  0E0C2455816B4242 CRC64;
     MKYNIKWDLE SIFPGGSSSP QLKEKLALIR NQLDELSLLT TKWDTEKDGP AFKELADILL
     VQEKLTKGLS QVFTFVEAVQ SADVLDKQAG ALLGQVIELS SAFSTLQIIL TKKMVAMPDN
     NWNELVKLPA FKEIEFSLNE TRRHGKELLS ETEEALINAL SIDGFQGWSD HYDSLVATIE
     IPFEDGEGHI HQLSVGQAYN KMNTDPDAKV REQLFKKWEE TWGGMAPLFS DTLNHLAGFR
     LADYKAHGVK DFLKRPLEYN RMNQETLDTM WKAVSDNKKP FVDYLNRKAQ LLGKDKLSWQ
     DTEAPVIIGN ASAKVYPYDD GADFIVKNFR KFSGKMADFA QYAFDHSWIE AEDRGGKRPG
     GYCSELPESK ESRIFMTYAE SPSEVSTLAH ELGHAFHSHV MTDLPTLNQQ YAMNVAETAS
     TFAEMIIADA TVKEATSKEE KITLLDTKIQ NALAMFLNIH ARFLFETRFY NERQNGILTE
     DRLGELMEEA QKEAYQDSLS EYHPHFWASK LHFFIADVPF YNFPYTFGYL FSLGIYARSL
     EEGAGFEDKY IALLRDTASM STEDLAKKHL NADLTKPDFW EAGIAIMKND VDTFMSLTEE
     YVK
//
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