ID   H5YQX2_9BRAD            Unreviewed;       635 AA.
AC   H5YQX2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:EHR05510.1};
GN   ORFNames=Bra471DRAFT_06328 {ECO:0000313|EMBL:EHR05510.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR05510.1};
RN   [1] {ECO:0000313|EMBL:EHR05510.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR05510.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-2011) 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; CM001442; EHR05510.1; -; Genomic_DNA.
DR   RefSeq; WP_007614235.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5YQX2; -.
DR   HOGENOM; CLU_021290_3_0_5; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000005774; 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          158..226
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          378..618
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..28
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  70840 MW;  282CC3E65E176949 CRC64;
     MNSRSKPALK KSALKKSALR KPATKKSVVK AKSSKPSPAK PASKTGKLPE WNLADLYSGI
     DAPEVARDLE RMDADCVAFE TDYKGKLATG TAKEDGGKWL AEAVRRYEAI DDLAGRLGSY
     AGLVHAGDSV DPKISKFYGD VSERLTAAST HLLFFALELN RVDDDILNRA MQATELAHYR
     PWIEDLRKEK PYQLDDKLEQ LFLEKAQTGY SAFNRLFDQT ISSLRFKVGP KELAIEPTLN
     LLQDRDGAKR KAAAEALAKT FKANERTFAL ITNTLAKDKD ISDSWRGFKD VADSRHLNNR
     VEREVVDALV ASVRAAYPKL SHRYYALKAR WFGRKRLAYW DRNAPLPFAA TDVIGWGDAR
     SMVLSAYRGF SPKMADIAER FFTDRWIDAP VRPGKAPGAF SHPTTPSAHP YVLMNYQGKP
     RDVMTLAHEL GHGVHQVLAA RNGALMAPTP LTLAETASVF GEMLTFRRLL AQTRSAKQRQ
     ALLAGKVEDM INTVVRQIAF YSFERAVHTE RKNGELTATR LGEIWLSVQG ESLGPAIEIK
     AGYENYWMYI PHFIHSPFYV YAYAFGDCLV NSLYAVYENA AEGFAERYLD MLAAGGTKHY
     SELLRPFGLD AKDPKFWDGG LSVIAGMIDE LEAMG
//