ID M5P4L7_9BACI Unreviewed; 1435 AA.
AC M5P4L7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Bacillopeptidase F {ECO:0000313|EMBL:EME74388.1};
GN ORFNames=BSONL12_11381 {ECO:0000313|EMBL:EME74388.1};
OS Bacillus sonorensis L12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1274524 {ECO:0000313|EMBL:EME74388.1, ECO:0000313|Proteomes:UP000011907};
RN [1] {ECO:0000313|EMBL:EME74388.1, ECO:0000313|Proteomes:UP000011907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EME74388.1,
RC ECO:0000313|Proteomes:UP000011907};
RX PubMed=23538904;
RA Adimpong D.B., Sorensen K.I., Nielsen D.S., Thorsen L., Rasmussen T.B.,
RA Derkx P.M., Jespersen L.;
RT "Draft Whole-Genome Sequence of Bacillus sonorensis Strain L12, a Source of
RT Nonribosomal Lipopeptides.";
RL Genome Announc. 1:E0009713-E0009713(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:EME74388.1}.
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DR EMBL; AOFM01000007; EME74388.1; -; Genomic_DNA.
DR RefSeq; WP_006638264.1; NZ_AOFM01000007.1.
DR STRING; 1274524.BSONL12_11381; -.
DR GeneID; 79845862; -.
DR PATRIC; fig|1274524.3.peg.2459; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4412; Bacteria.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000011907; Unassembled WGS sequence.
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 NCBIfam; NF038128; choice_anch_J; 1.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF13620; CarboxypepD_reg; 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..1435
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004069287"
FT DOMAIN 70..178
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 216..502
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 791..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 450
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR015477-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1435 AA; 155800 MW; 624B0D58A451F2EB CRC64;
MKRKLKKKAL CSILSGLLAG SMLMPAASSA AESASPLTSY KEQAKQNAST GKKISASLVK
RFKKEDMVTF LIKMKDQVDT QKVAKQAEKK AKAKSLSSAK AEYQKRSAVV SSLRIKADET
QERLQSYLKK QAKKGNAKDI HSFYIVNGMA VRATKEVMEQ VAAFPEVEKV LPNEKRQLIK
PAKQSVKQKP VQARGGIEWN IDQISAPKAW GLGFDGTGTV VASIDTGVEW DHPALKEKYR
GYDPAHPDSP DHEFNWFDAT TGGSEPYDDL EHGTHVTGTM VGSESGGQNQ IGVAPGAKWI
AVKAFNEDGG TDEDLLEAGE WILAPKDKDG NPHPEMAPDV VNNSWSGGSG LDEWYRDMVK
AWRAADIFPE FSAGNVDLFN PGGPGSIANP ANYPEAFATG ATDINKQLGD FSLLGPSPYD
ETKPEITAPG VNIRSSVPGK GYQDGWDGTS MAGPHVSAVA ALLKQADASL SVDEMEQILI
NTATPLTDSK FTESPNNGYG HGLVNAYEAV SAVTEGLGKA EGRVGKEGED SKPPVLTHEP
FKEVFSGSDI SFTAEAEDDV SIATVKLAYQ IDSSEWRTVA GKQISGDYKK GTFEAVIPSL
DGKILSYKWI VTDFGGNQTE SNLYEVPISF AVTTGYKQSF ETPAAGWTSY GVNDSWQQGV
PESGPKSAAS GKQVYATNLT GPYQDSANMN LLMPKVQVPK NQKLYLHFKY WHEFEEDFDY
GFVYIQPEGE TEWVQAAQFT GVTPDWMDEE IDLSQYQGQS IKIMFNLQSD EDISKDGLYI
DDVELVKEPK STGKKNRLGV EKRTGSMKDK KTKKQTIDPK QAKPADAVRQ DIQRGKASPA
VLPLRAKVSV LETGKSTYSS ENDGSYSIAH LPGTYTIKAE AYGYESSTQT VKIEADKTTT
ADFVMKELKK ATLKGIVKNK KSGEPVRHAK IYLIEDAAVK PVQTDENGTY SITAYENSYT
VKIAAKGYYS SQFTVDLKGD ATRDIELDPY IGYPGEIGYD DGTAENAWAF YEADNAIAVK
MSLDKGQEQA MLKGGLFKFW EADFPDPGGT DFAVEVYDAS GEKGSPGNKI AGPFTGEALR
NGEWTNVDLS DEGIMVGKDF YLVYVQTKDM DHSPALASDE DGENSGRNWQ FTDGAWSKIP
VEQGNFMIRA LVDYEVSVPV ITSPKDGLVT NQKKTVIEGT SSPTITVHLF NGKEEIGTVQ
TGKDGTFSKE IALQKGENII TAKASAASGT TDASAPVRIV LDQTKPKLSI TAPEDGSKLN
KETVTVTGTV SDDHLDSVKV NGKKAAVENG EYSARILLDN GKNEIKVTAA DAAGNKTTKK
VAVDVNFEGP QITNLKPAED IQLKTGETVK IEFESTADLD AVFVVRMPLT NFKTAAQNVT
ELPLREVSSG KYEGYWTATS TAKAKGAEIE VIACDDYGNE VRKTAKGKLY INEKS
//
