ID Q11ER8_CHESB Unreviewed; 616 AA.
AC Q11ER8;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:ABG64107.1};
GN OrderedLocusNames=Meso_2730 {ECO:0000313|EMBL:ABG64107.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG64107.1};
RN [1] {ECO:0000313|EMBL:ABG64107.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG64107.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) 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; CP000390; ABG64107.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11ER8; -.
DR STRING; 266779.Meso_2730; -.
DR KEGG; mes:Meso_2730; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_0_5; -.
DR OrthoDB; 9766487at2; -.
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 136..205
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 220..599
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 616 AA; 69272 MW; 4263D666DDDD7F70 CRC64;
MAHYPKTPAG LAQATEAGAR KADLGALPEW NLADLYPSMD STEFSEDLAR AAREATAFEQ
NWKGRLAEEA GKGTSGRLGE AVREYEALDE LFGRIGSYAG LLYTGDTSDP KRAKFYGDVQ
EKLTDASTHL LFFTLELNKI DDALIEAAMK DDPIFGHYRP WVLDIRKYRP HQLEDSIERL
FHESDVTGRG AWNRLFDETM TGLRFDVDGE ELTLEPTLNL MQDPDGEKRR KAAAALAVTL
KDNMRLFTLI TNTLAKDKEI SDRWRNFADV ADSRHLSNRV EREVVEALAA SVCAAFPRIS
HRYYAMKAKW LGMEKLNHWD RNAPLPETPQ SVIGWDEAKE TVLSAYASFA PEMADIAKHF
FDRNWIDAPV RPGKSPGAFA HPTVPSVHPY VMLNYMGKPR DVMTLAHELG HGVHQVLAAG
QGSLMAATPL TLAETASVFG EMLTFRSLLA RTTDKRERKA MLAQKAEDMI NTVVRQIAFY
EFERKVHTER RQGELTADRI GEIWLEVQAE SLGPAIALRE GYETFWAYIP HFIHSPFYVY
AYAFGDCLVN SLFAVYQQAE KGFQEKYFEM LKAGGTKHHS ELLAPFGLDA SDPAFWTKGL
SVIESLIDEL EALEEG
//
