ID D2D3C3_BACAM Unreviewed; 1431 AA.
AC D2D3C3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Bacillopeptidase {ECO:0000313|EMBL:ACO07296.2};
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390 {ECO:0000313|EMBL:ACO07296.2};
RN [1] {ECO:0000313|EMBL:ACO07296.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CH86-1 {ECO:0000313|EMBL:ACO07296.2};
RA Kwon G.-H., Lee H.-A., Lee A.R., Kim G.M., Lee K.W., Kim J.H.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACO07296.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CH86-1 {ECO:0000313|EMBL:ACO07296.2};
RX PubMed=21617349;
RA Kwon G.H., Park J.Y., Kim J.S., Lim J., Park C.S., Kwon D.Y., Kim J.H.;
RT "Cloning and expression of a bpr gene encoding Bacillopeptidase F from
RT Bacillus amyloliquefaciens CH86-1.";
RL J. Microbiol. Biotechnol. 21:515-518(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; FJ432003; ACO07296.2; -; Genomic_DNA.
DR MEROPS; S08.017; -.
DR GO; GO:0008233; F:peptidase activity; IDA:CACAO.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07481; Peptidases_S8_BacillopeptidaseF-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR033857; Bacillopeptidase_F.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR012103; Pept_S8A_Bpr.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF13715; CarbopepD_reg_2; 2.
DR Pfam; PF09136; Glucodextran_B; 2.
DR Pfam; PF20773; InhA-like_MAM; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF015477; Bpr; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003029753"
FT DOMAIN 69..177
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 220..506
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 794..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..820
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 454
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1431 AA; 154513 MW; B56B9AD6DFD2E243 CRC64;
MKKKTRNRWT GSVLSAIVVS SLLFPGAAGA NSTPGAVSFT KDLSSSKSIQ HKISDSVKKR
FEKNDKVTFL IKFKEKANTK KAVKEAEKNA KSQSLSAAKT EYQKRSAVVS SLKLAAHDAQ
QNLKTYLEKQ KKKGKADHIH SYYIVNGMAV TASKEVMEKA ASFPEVEKVL PNEKRQLTQR
QSKAPFQMKK KQKEIKAKEG IEWNISQIDA PQAWASGYDG TGTVVASIDT GVQWEHPALK
EKYRGYDPEN PAKPNHEMNW YDAVSHKDAP YDDLEHGTHV TGTMTGSEPD GSNQIGVAPG
AKWIAVKAFS DDGGTDADIL DAGEWVLAPK DKNGTPHPEM APDVVNNSWA GGSGMDEWYR
DMVNAWRAAG IFPEFSAGNE DLFTPGGPGS IANPANYPET FATGATDIDK KLADFSLQGP
SPYHETKPDI SAPGVNIRSS IPGGTYEGGW DGTSMAGPHV AATAALLRQA NASITVDEME
DVLTRTAEKL TDSVFPESPN NGYGHGLVNA FDAVSAVTDG IGSVAGKVSS AGEDHNPPSF
HHEPVSAAYK GANLPLTVTA EDDVSVTEVI LSYQFDEGEW KTTAAVQKSG DEKKGTYQAE
IPDVTGSKIS YKWTIKDFGG HSVESDTYRA DVKPSVTAGY KEDFESQPAG WSSYGTHDQW
EWGTPGSGPG TAFSGDKVYA TNLSGPYADS ANMNLVMPPI QVPETGRLFL QFKSWHKLEE
FFDYGYVFVL PEGKSNWEQA AVYNGDSAGW NDEEADLSAY KGQNIKLMLN MQSDEVLNED
GWYIDDVRLS SSPLGKAAKK NKHKRQPPPG HLKKKAVSPK QAKPAVKSPG KRVKRETNLL
PLRAQISVSE TGKSVYSDPA SGSYSLSHKA GSYTLKAEAY GFKSASKQVS IQSDKTAQAD
FTLEQMPSGT LKGTITNQST GEPVKGAALY VAEDAAIEPA VTNDKGEYSL KAYEGSYTIK
VAAKGFYNSE FSVDIKGDAE KNVKLKPYIG YEGEIAYDNG TEEAALSYFK AGSKSAVKMT
LKDGKEHGML TGGLFKFWGA DWPDPGGTEF QAEVYDASGP DGAPGSKIAG PFQAEALRNG
EWTKVDLSSK GIAVGKNFYL VFRQTKPDPY TPALSSDDGS PYSNRNWQYL DGRWSKTDKS
DGNFMIRALV DYEASVPDIT SPEDRSFTNK RSITVKGTAS PKTAVRLTNN GKTAAETKAD
ADGNFQAGVT LTEDANRLTA ASVTDSGSTD ESRPVTVILD EDKPDVTIDS PANGDKTNKE
AVTVKGKVHD AHLEWVKVNG KKAEVNNGSY QARTLLENGS NEIKVTASDE AGNKTTKKTV
IDVNYNAPVI SGLVPGADKE LKAGESVKIA FSSGKKLDAS FVIRLPLTNA RAGSQNATEL
PLREIFPGRY EGYWTATSSI KASGAKIDVI ARDDYGNETR QTAKGKLYIN E
//
