ID A0A0M2PI53_9BACI Unreviewed; 610 AA.
AC A0A0M2PI53;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Oligoendopeptidase F {ECO:0008006|Google:ProtNLM};
GN ORFNames=WQ54_11175 {ECO:0000313|EMBL:KKI92129.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI92129.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI92129.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI92129.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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}.
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:KKI92129.1}.
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DR EMBL; LATZ01000015; KKI92129.1; -; Genomic_DNA.
DR RefSeq; WP_046516362.1; NZ_LATZ01000015.1.
DR AlphaFoldDB; A0A0M2PI53; -.
DR PATRIC; fig|1455638.3.peg.2461; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000034887; 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 Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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 PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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 113..181
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 205..589
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 610 AA; 69845 MW; 5A8EE2B559FD8CCB CRC64;
MNLVTRKDVP EEDTWNLTDI FPSDIEFGRA YSAAEQEIDE MLSGKISLSS AFETLNSIRK
YDNLMERLHR ISSYAMFKYS EDESDPDSQK LMGRAQLLVG KGNKVSTKFV NILIQIPKEA
MTKYLEEEKD LQLYNRFLQR IDETRQHALT PDMEEILASL GQSLKSPETF YLTITSSDLK
FEPVKDKNGN EVPVSLHMYM TQIETSPDTT LRRNAYKSLT KGLKSHQHGL AKILSSEINK
NVSLAKLRGF SSALDMHLQF SPASTNFYTT DEISTEFFEQ ILDIFQNELS PYMQRYARLR
KKQLGLDTLL LSDVKAPLDP EFDPPISYKE AGEIITEAVG VLGSEYQNQM RKAFSERWVY
RGDNIGRRMI AFGGGVHGVH GYSFYPWGGN LFDMLLLSHE LGHTIHYTLS AQNQRYINNS
QSMLFVESPS TLIEHLVVHY LQEQRSDPRL NRWLNMYLMM SYHHNCVTHV LEAELLRRLY
KMAENKEPLT TLDISQTKGK ILTEFWGDTV EIDDGAILTW MRQPHYYMGL YPFTYSVGIS
AATIIAQRIK TEGIGIGEQW TKVLKQGGNM KGLDLYKMAD LDMSTTSIIK ETITHVGTIV
DNLEKSFSLS
//
