ID W7UI05_RUMFL Unreviewed; 334 AA.
AC W7UI05;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Peptidase M42 family protein {ECO:0000313|EMBL:EWM54851.1};
GN ORFNames=RF007C_10965 {ECO:0000313|EMBL:EWM54851.1};
OS Ruminococcus flavefaciens 007c.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1341157 {ECO:0000313|EMBL:EWM54851.1, ECO:0000313|Proteomes:UP000019365};
RN [1] {ECO:0000313|EMBL:EWM54851.1, ECO:0000313|Proteomes:UP000019365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=007c {ECO:0000313|EMBL:EWM54851.1,
RC ECO:0000313|Proteomes:UP000019365};
RX PubMed=24992679;
RA Dassa B., Borovok I., Ruimy-Israeli V., Lamed R., Flint H.J., Duncan S.H.,
RA Henrissat B., Coutinho P., Morrison M., Mosoni P., Yeoman C.J., White B.A.,
RA Bayer E.A.;
RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT comparative genome-wide analysis of six ruminococcal strains.";
RL PLoS ONE 9:E99221-E99221(2014).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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:EWM54851.1}.
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DR EMBL; ATAX01000008; EWM54851.1; -; Genomic_DNA.
DR RefSeq; WP_037296856.1; NZ_ATAX01000008.1.
DR AlphaFoldDB; W7UI05; -.
DR PATRIC; fig|1341157.4.peg.467; -.
DR eggNOG; COG1363; Bacteria.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000019365; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF5; ENDOGLUCANASE; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019365}.
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 334 AA; 36284 MW; 4CB7B9EFA92CAC2D CRC64;
MKELLKELCL TDGISGDESA VRDLIISKIK DVCQYSIDNL GNLICFKKGS KSPEKKLMIC
AHMDEVGFMV TYIRSDGTLS FGNVGGIDPS VVIGRPVRVG KDRISGVIGS TAVHNLSKEQ
REKAPKTDSL YIDIGAKDKA DAEKYVSLGD CVYFDSEFTE LGQHRVKGKA IDDRAGCAIM
IKLLHEKLDY DTYFVFNVQE EIGLRGSAVS SFSVAPDYAI VLEATTAADI DGVSGEKRVC
ELGSGPVVSF MDRSTIYDKE LYQLAFAIAT CQTKTMIAGG NDAGAIHISG KGVRTIAISV
PCRYLHSPSS VIELSDLTSS YKLVKNLLKR IPEL
//
