ID F0SU08_SYNGF Unreviewed; 440 AA.
AC F0SU08;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Processing peptidase {ECO:0000313|EMBL:ADY56531.1};
DE EC=3.4.24.64 {ECO:0000313|EMBL:ADY56531.1};
GN OrderedLocusNames=Sgly_2242 {ECO:0000313|EMBL:ADY56531.1};
OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Syntrophobotulus.
OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY56531.1, ECO:0000313|Proteomes:UP000007488};
RN [1] {ECO:0000313|EMBL:ADY56531.1, ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX PubMed=21886864;
RA Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT (FlGlyR).";
RL Stand. Genomic Sci. 4:371-380(2011).
RN [2] {ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP002547; ADY56531.1; -; Genomic_DNA.
DR AlphaFoldDB; F0SU08; -.
DR STRING; 645991.Sgly_2242; -.
DR MEROPS; M16.A15; -.
DR KEGG; sgy:Sgly_2242; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_0_9; -.
DR Proteomes; UP000007488; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ADY56531.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007488}.
FT DOMAIN 33..180
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 186..358
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 440 AA; 49842 MW; 717C0B4746B98FEA CRC64;
MKKGLLLCSM NEESDFGGIE QLYQKVVLPN GVRVLTEEID YLRSAAIGIW VGAGSRYEKS
GYEGISHFIE HMFFKGTKKR TARQLAESLE SVGGQLNAFT TKEMTCYYAK VLDEDIDLAI
DVLSDMFFHS LFDPKEIEKE KNVVLEEVKM YLDTPDELIH DLFSQYIWNE HPLGMPILGD
EGSIKSLDRD KIMDYLETQY CPDKIVISAA GKIKHDHIGK SLEQFGSFER QKEVSVYCHP
VAKVIRTSMP KDTEQMHLVL GVPGIGQNDE DMYALHVINN ILGGGLSSRL FQEIREQRGL
AYSVYSYHAT YVDTGLFAVY AGASPGNIEE VIKCILHEIN GIRSKGLSEE ELRRVVAQIK
GNLYLGMESS SSIMSRLGKT ELSFDRVKTA EETVEKLEKV TLKDIDRVME RLWHKDKVSM
LTIGSKEFTP DFDQIINAQF
//
