ID D4LZ73_9FIRM Unreviewed; 343 AA.
AC D4LZ73;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=RTO_26190 {ECO:0000313|EMBL:CBL27083.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL27083.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL27083.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL27083.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL27083.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL27083.1,
RC ECO:0000313|Proteomes:UP000008956};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU362031};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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DR EMBL; FP929055; CBL27083.1; -; Genomic_DNA.
DR AlphaFoldDB; D4LZ73; -.
DR STRING; 33039.ERS852502_01378; -.
DR KEGG; rto:RTO_26190; -.
DR PATRIC; fig|657313.3.peg.2499; -.
DR HOGENOM; CLU_025778_1_3_9; -.
DR Proteomes; UP000008956; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW Metal-binding {ECO:0000256|RuleBase:RU362031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU362031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CBL27083.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362031};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT TRANSMEM 84..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 6..330
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 343 AA; 37214 MW; 9F4EF2E27577EC36 CRC64;
MGIILAILLF SAIVIFHELG HFLLAKKNKI RVDEFSLGLG PTIFGKQFGE TKFSLKLLPF
GGACMMGEDD VDDMSEGSFN SKSVWARMSV IVAGPVFNLI LAWILCMIII GWTGYRAPIV
SNVTDGYSAQ EEGIEPGDVI KKIGGKSVYI WNDISLYNMM HAGTKSVEVE YERDGKDYTV
VLEPKQNAGD AFPLLGITGG EMVRPGLFGT VRYGAYTVKY WITYTVDSLK MLVGGKVGVK
DLSGPVGIVS AVDNVYQEAA PAGMVVVILN LLNIGVLLTA NLGVMNLLPL PALDGGRLVF
LIIEAVRGKR VPPEKEGMVH FAGFVLLMAL MVVIMFNDIL KLV
//
