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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//