ID V6IW63_9BACL Unreviewed; 595 AA.
AC V6IW63;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Oligoendopeptidase {ECO:0000313|EMBL:EST11472.1};
GN ORFNames=P343_11975 {ECO:0000313|EMBL:EST11472.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST11472.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST11472.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST11472.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(2013).
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 -!- 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:EST11472.1}.
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DR EMBL; AWTC01000011; EST11472.1; -; Genomic_DNA.
DR RefSeq; WP_023510638.1; NZ_AWTC01000011.1.
DR AlphaFoldDB; V6IW63; -.
DR STRING; 1395513.P343_11975; -.
DR MEROPS; M03.A08; -.
DR PATRIC; fig|1395513.3.peg.2425; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000018296; 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 Reference proteome {ECO:0000313|Proteomes:UP000018296};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 117..180
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 201..580
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 595 AA; 68588 MW; DDEEDB5E76237371 CRC64;
MEKLNQQWDL ESIFQSGSKS DEFQDFLNSL TESISRFRSE LELKTIPFTV NEAQAFSRLV
RTYETLTKQF HEAHAYVECL TAQNIKDVNA SLANNRIQSL GAELNACDSL FENILRQISD
LSWSELLKNS DLKEVQFALR EKREISKKKL SSDQEQLISG LAVDGYHAWE DLYYSLIGKM
HIDLEKDGKN ETLSVSQANN LLDDADRNVR GKAFEALESA WSEYADLFAA ALNHIAGYRI
AAYKARGWEN ILDEPLDYNR MSEQTLTTMW TEINKYKPKL ATFMERKAQL LGLKKLSWYD
VDAPLSKNSS KLTYEDAADF IIEHFQSFNP KMASFAKEAL ENRWIEAENR ADKRPGGFCT
NFPIAEQSRI FMTFSGTASN RSTLAHELGH AYHQSLMNKL PYLSQNYAMN VAETASTFSE
MIVSDAAQAV AKTKEERINF LADKLERCVA LLMNIHARFL FETRFYAERK QGVVSVKRLN
QLMIDAQREA YLDSLDVYHP TFWASKLHFF ITDWPFYNFP YTFGFLFSTG IYVQALQEGP
KFADRYDALL RDTGRMTTEE LAEKHLNVDL TKPAFWQSAL DYIMRDVDEF LELTE
//