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Database: UniProt
Entry: A0A161I926_9MICO
LinkDB: A0A161I926_9MICO
Original site: A0A161I926_9MICO 
ID   A0A161I926_9MICO        Unreviewed;       844 AA.
AC   A0A161I926;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Bacillopeptidase F {ECO:0000313|EMBL:ANC32358.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:ANC32358.1};
GN   Name=bpr {ECO:0000313|EMBL:ANC32358.1};
GN   ORFNames=I598_2839 {ECO:0000313|EMBL:ANC32358.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC32358.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC32358.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC32358.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CP014209; ANC32358.1; -; Genomic_DNA.
DR   RefSeq; WP_068203490.1; NZ_CP014209.1.
DR   AlphaFoldDB; A0A161I926; -.
DR   STRING; 1300344.I598_2839; -.
DR   KEGG; ido:I598_2839; -.
DR   PATRIC; fig|1300344.3.peg.2857; -.
DR   OrthoDB; 9813435at2; -.
DR   Proteomes; UP000076794; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 2.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
DR   PROSITE; PS51318; TAT; 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:UP000076794};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..844
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039725808"
FT   DOMAIN          193..438
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        248
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        418
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   844 AA;  86651 MW;  FD314E5DD743C883 CRC64;
     MHQSRPPGRR RAAWTVATLT AAALLTGPLT AAADTAGPLA DSPKVDPALA SAVSDGAEAT
     FFVVLKDQAD LAAPRAKRSH AAKAEAAYDE LREHAASSQK SLTAFLDRKK VGHEDFWIAN
     TVQVTGDADL VAELSKRSDV ASVVPEQTYY LDATEASPAG DVESERATTA AAPEWGVADI
     NADDVWAQYE DRGEGIVIAN IDSGVQYDHP DLVGTYRGND GDGTFTHDYN FYDPTGTCTD
     GPCDNNGHGT HTMGTMVGAN GIGVAPGATW IAAKGCEARS CSDASLLKAG QWILAPTDAE
     GLNPRPDLAP NIVNNSWGGG RTTFYQDIVE AWNAVGIFEA FAAGNSGDGA TCSTTESPGA
     QAPAYGVGAY DVTGTIADFS GFGPSPVDGS AKPNIAAPGV NVRSTVPGSA YQANNGTSMA
     TPHVAGAVAL LWAASPALIG DIAGTRELLD AGARDVDDTH CGGTAAMNNV WGEGKLDVLA
     SVELAPRTAG TLTGTVKEKG TGTPLEGVTV TAENAAGVRS VVTGPDGTYR LNLVPGTYDV
     TMRGYGYATR TFTGIEVTDG ATTKRGAQLA ATAQHAVTGT VLDVTGAPLA GATVQVEGAP
     LAAVTTGADG SFQVPAVAEG DYALVATPAE PVLCNGTSRT DLTVDGAEAR TVQLPAKADF
     FGNSCTPVEY SWVKGASTVA LSGDEDAATI SLPFWVSLYG VDYSSASVTT NGLVNFLSPR
     LGDYENTALP EAAAPNGVVA PFWDDLMLDK RSSVQTATKG KAGNRTFAIV WNKAVLVDDG
     GRVTFEVLFH EASGDVTFQY QSVPGSGASA TVGIENQTGA DALQYSFDQP VLTDGSAIRI
     TPGA
//
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