ID E8RQB4_ASTEC Unreviewed; 607 AA.
AC E8RQB4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Oligoendopeptidase, pepF/M3 family {ECO:0000313|EMBL:ADU13216.1};
GN OrderedLocusNames=Astex_1550 {ECO:0000313|EMBL:ADU13216.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU13216.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-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; CP002395; ADU13216.1; -; Genomic_DNA.
DR RefSeq; WP_013479048.1; NC_014816.1.
DR AlphaFoldDB; E8RQB4; -.
DR STRING; 573065.Astex_1550; -.
DR KEGG; aex:Astex_1550; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_3_0_5; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000001492; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000001492};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 127..194
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 215..592
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 607 AA; 67398 MW; 7094E890917B00CB CRC64;
MTQTASTDSA PTLSNALPVW DLTDLYSSVD DPKIAADFAE ATATLKELQK LQGNFVAARG
NAERLGLLID QAATLYERAS DRMAGAMAYT TLASTISRED TRIAKLDADL RNKAALISTD
SLFLSLELNQ LEDWEIEQAL RVTEKAQKWR PWLRRIRANR PHELSADLEK LLLEKMPGAT
SWVRLFDETL TRLRVKIGPK SKPEVLTLNE ALTRLSSPDE AVRKAAAEGL SVALKDNAPV
LALALNTLAF EKQVEDRWRK FATPAASRHL ANEVDGDGVD AMAEAVGESY AALSHRYYAL
KAKVMGKTVL NFWDRNAPLT AAAPKLYSWD EARSIVLDSF ARLGPDFAER AAVFFEKPWI
DAQPREGKSS GAYAHPVSSS HHPYVMLNFT GERREMLTLA HELGHAVHQT LAAPLGSILA
DTPLTLAETA SIFAEGLVFE YLVADASPED KKALLAGKIE DGLNSVVRQI AFHRFEERFH
AERLEGEVPV DRLNALWLEV MGESLGPAIT LNDGYEYWWA YISHFVHAPF YVYAYAFGDL
LVSALMEKRR ENPEAFTPLY AQLLSAGGTK TYVEALAPFG LNPREKAFWE MGCQRLKGLI
DQFEALV
//
