ID I2GR79_9BACT Unreviewed; 578 AA.
AC I2GR79;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Oligoendopeptidase, M3 family {ECO:0000313|EMBL:CCH56407.1};
GN ORFNames=BN8_05741 {ECO:0000313|EMBL:CCH56407.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH56407.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH56407.1, ECO:0000313|Proteomes:UP000009309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309};
RX PubMed=22843583; DOI=10.1128/jb.00869-12;
RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T.";
RL J. Bacteriol. 194:4445-4445(2012).
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:CCH56407.1}.
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DR EMBL; CAIT01000009; CCH56407.1; -; Genomic_DNA.
DR RefSeq; WP_009284972.1; NZ_CAIT01000009.1.
DR AlphaFoldDB; I2GR79; -.
DR STRING; 1185876.BN8_05741; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9762795at2; -.
DR Proteomes; UP000009309; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09606; M3B_PepF; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR NCBIfam; TIGR02289; M3_not_pepF; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF48; PUTATIVE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000009309};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 178..557
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 578 AA; 67228 MW; 9F286C016B943ED0 CRC64;
MIQDTTLEIP TRPSRPFIGE EMELKSWEDV RPFYDNLLNR PIENADDLHQ WLLDRSELES
YLSENFAWRY IRMTCDTSNE DLISKLNFFI ADIQPQMTAY GNDLDLKAVN SPFLSQLTDA
GYDVMVRSMK KAIEIFREEN IPLQTEMQTE ERKYGAIAGA MTVVIDGKEV TLQQASDLLQ
STDRAVREEA WRKIWERRYE DHESLDELFD RLRTLRHQVA VNAGFANFRD YAFAALGRFD
YTPDDCFNFH ESVAAAVVPL LDTLANERKQ KLSVDPLRPW DSKVDPDGHP PLKPFTTSNE
LLEKTIACFD RLDVQLGNYL RIMRAMGHLD LESRKGKAPG GYNYPLEEIG VPFIFMNATS
SLRDLVTMVH EGGHAVHSFL TRELPLKAFR NPPMEVAELA SMSMELLSMD HWDVFFDNPE
ELRRAKLQHL ESIIETLPWV ATIDKFQHWI YENPTHSITE REQNWLQIYD QFSDNVTDWS
GLESFNAYVW QRQLHLYEVP FYYIEYGIAQ LGAIGIWRNY RKDPATGLQG YKDALSLGYK
APIRAIYDAA QVPFDFSRQH IQELIGFVWE EIEQLKKS
//