ID I8U9T2_9BACI Unreviewed; 1408 AA.
AC I8U9T2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Bacillopeptidase F {ECO:0000313|EMBL:EIT83715.1};
GN ORFNames=A374_19385 {ECO:0000313|EMBL:EIT83715.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT83715.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT83715.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT83715.1,
RC ECO:0000313|Proteomes:UP000004080};
RX PubMed=22887677; DOI=10.1128/JB.01049-12;
RA Cai L., Zhang T.;
RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL J. Bacteriol. 194:4780-4780(2012).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC 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:EIT83715.1}.
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DR EMBL; AKKV01000053; EIT83715.1; -; Genomic_DNA.
DR STRING; 1196324.A374_19385; -.
DR PATRIC; fig|1196324.3.peg.3939; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4412; Bacteria.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000004080; 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; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR NCBIfam; NF038128; choice_anch_J; 1.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF13715; CarbopepD_reg_2; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF09136; Glucodextran_B; 2.
DR Pfam; PF20773; InhA-like_MAM; 1.
DR Pfam; PF00082; Peptidase_S8; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004080};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003714861"
FT DOMAIN 210..495
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1408 AA; 151949 MW; B94222555A2F38D2 CRC64;
MKGKFMSVIM TACLSLSLLF PSGAAVSATS KMKAYHGMNA IKATQVEKVS NKLLKEFKDK
KIATFLVKFK EQVDAEKEAK KAMMSAQKKK MSSYQTELMK RSAVVSTLQA KALESQKEVS
SYLEEQKKKG EVKKIHAFFI VNAMAVTATK AVMDKLATMP EVEKITANEV RKLQPVQSPK
KKATSKESNT IEWNVQKVDA PKAWAKGIDG TGTVIASIDT GVEATHPAIA SKYRGYDAGG
KLHNEYNWFD ATEGEDQPYD DIGHGTHTVG TMVGSEKNGK NKIGVAPGAK WIAVKAFTEE
GGTDEALLAA GQWVIAPTDA AGKPHPEKAP DVVNNSWGGG PGMDDWYRPM VKAWRAAEIF
PEFSAGNTDA NNEGGRGSVA NPANYPESFA TGAVNDKNQV ADFSLRGPSP YEGLLKPEVS
APGVNIRSSV PGGKYEDGWD GTSMAGPHVS AIAAMLRQVN HSLTVKEMEE IIKNTATPLT
DKEYPKSPNN GYGAGLVNAY EAVNAVTKGL GKVTGVVTKD GNDTKAPVFK HEAVKTASEG
ITLPLTIDVQ DDVSVVAVTL QYSDGKGGWK ERPAELVNGS VRSGTYAAEI PNKEMTAPSL
AYRFKIKDFG KHEVTSDPYH VTVTPSIKVG YETDFEKQPA GWRTFGVNNN WEWGVPKSGP
KSAASGTHVY GTNLKGLYAN SADMFLMMPS VKVEKGSTFL QFKHWFEFEK DMDGGAVIVS
TDEKQWNYVK MYTGKSRKWV DGEVDLSDYA GMTVSVGFEV RTDEQNAFPG WYLDDVKLSS
VALPKGKVAT DAFTPKKPFA KLAKEKPTLQ KATVEANSGI PMEANVSLLE SGKSTVTNPA
TGEYTLYGSP GNYTLAIDAY GYTPMKQKVQ IDAKKETSQS FKLKEKAKGT LSGKVTNAQT
GKPVAKAVVY VLEDGAVTPV LTDQNGVYHL TAYEGNYTLR IGGAGYYSQE VSVTLGKQAV
KDIQLKPFLS APGKEIGYDD GSEENAVAFF DPNNYWAVKM SLPKGKTKAM VTGGMYKFSE
SFPMPGGTEM QAAVYDASGK DGAPGKRIAG PINATALRNG EWTKVDFGGQ SVQVSGDFYI
VSIQTKKDIE SPGIAADLNS PSANRGFTYV NGVWEPFPSS EGNLMIRALV EYEVTAPMIT
KPTNASFTNL ETYTVEGTTA PTIKVALMND GKQVSQVTSD KKGKFKAPVK LHKGKNVLST
KAVFDRGSTE VSAPVVITLD RTPPKLTITS PSNGIKTNKE TVTITGTASD DFMKSVTING
ENVSLQSKGK FEHRLMLQSG KNQIRTTVVD RAGNATVKEL TIYAQFKGLA LTNMKPARNV
TLKAGQTLKV ECDTLTRSSA SFLLRLPLST VSNKQATMKM KETTAGHYVG YYKVPKNVKA
SDIAIEISVK DSFGNTTTKL APGRLTIQ
//
