ID F7Y953_MESOW Unreviewed; 612 AA.
AC F7Y953;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:AEH86425.1};
GN OrderedLocusNames=Mesop_1944 {ECO:0000313|EMBL:AEH86425.1};
OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH86425.1, ECO:0000313|Proteomes:UP000001623};
RN [1] {ECO:0000313|EMBL:AEH86425.1, ECO:0000313|Proteomes:UP000001623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC {ECO:0000313|Proteomes:UP000001623};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P.,
RA Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP002279; AEH86425.1; -; Genomic_DNA.
DR RefSeq; WP_013893150.1; NC_015675.1.
DR AlphaFoldDB; F7Y953; -.
DR STRING; 536019.Mesop_1944; -.
DR KEGG; mop:Mesop_1944; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_0_5; -.
DR Proteomes; UP000001623; Chromosome.
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; cd09610; 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; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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|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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 133..202
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 219..597
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 612 AA; 68730 MW; 41998BC2245C98DE CRC64;
MRMMFGRRLA APASGQGAAG LGDLPEWNLA DLYTGMDAPE LKRDIARAAA DAIAFEARWK
GTLAAEAERG SAGRLGEALV AYEALEELIG RIVSYAGLVY AGNTADPQRA KLYGDIQEKM
TDASAHLLFF ALELNLIDDA AIEGALAGDP AFGHYRPWVL DLRMDKPYQL EDRVEQLFHE
KSITGRGAWN RLFDETMTDL RFDVDGEELT LEPALNRLQD ADGEVRRRAS EALAATFRKN
LRTFTLITNT LAKDKEISDR WRGFEDIADS RHLANRVERS VVDALATAVR EAYPRLSHRY
YQMKARWLGM EVMNHWDRNA PLPETPQAVI GWDEARNTVL SAYQRFSPDM AEIARTFFDR
NWIDAPVRPG KSPGAFAHPT VPSAHPYVLL NYMGKPRDVM TLAHELGHGV HQVLAAGQGA
LMASTPLTLA ETASVFGEML TFRSLLEQTT DRRERKAMLA QKVEDMINTV VRQIAFYEFE
RKVHAERRNG ELTSDRLGQF WLEVQAESLG PAIKLREGYE VFWTYIPHFI HSPFYVYAYA
FGDCLVNSLY AVYQNAERGF QDKYFEMLRA GGTKHHSELL APFGLDATDP AFWQIGLGVI
GGLIDELEAL DG
//