ID A0A087A0R4_9BIFI Unreviewed; 671 AA.
AC A0A087A0R4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KFI52364.1};
DE EC=3.4.21.107 {ECO:0000313|EMBL:KFI52364.1};
GN ORFNames=BCAL_2009 {ECO:0000313|EMBL:KFI52364.1};
OS Bifidobacterium callitrichos DSM 23973.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI52364.1, ECO:0000313|Proteomes:UP000029072};
RN [1] {ECO:0000313|EMBL:KFI52364.1, ECO:0000313|Proteomes:UP000029072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI52364.1,
RC ECO:0000313|Proteomes:UP000029072};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KFI52364.1}.
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DR EMBL; JGYS01000017; KFI52364.1; -; Genomic_DNA.
DR RefSeq; WP_043166615.1; NZ_JGYS01000017.1.
DR AlphaFoldDB; A0A087A0R4; -.
DR STRING; 1437609.BCAL_2009; -.
DR eggNOG; COG0265; Bacteria.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000029072; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KFI52364.1}.
FT DOMAIN 511..582
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 66297 MW; E5D368ECDB1CF62F CRC64;
MADEQNNWAP QGNQNAQPQR DAQETQHIPT PAGADSVKAA GEQPTETISP VAGGQGAAAA
ANGEVKPDYA SAAGEQTVVS SKPVSSSAPT ASAAQPTSTS AAAQQPSYGQ YRLAPEYGAY
GPVPTPQQQA GQTSQSNGQV NGQPGPFGAA GQNGQNPQGQ PQYGQRSGSI FGGSNPFASN
NPFASPNPGA GNGANGANGG NGSGNPFGGF PPFGGNGNNN GGNGNGQPGD PNQPIDPNQF
NQIGAKSSNG VGRLVVTGVV AALVSAALCL GVGYAAITSG AVRVATTSSL SNVDSSKSSS
GSATAKTGEA PDWQAVAKQV SGSVVAIQTQ LSNGSAKGSG AILDKDGHIV TNNHVISGAQ
KIQVTLSNGQ MYSAQIVGTD TTTDLAVIKL DNPPSDLKTV TFADSDELAV GENIMAVGNP
LGYDDTATTG IVSALNRPVT VMDDNNNDIV TNAVQIDAAI NPGNSGGPTF NAAGQVIGIN
SSIASTSSSS SSSSAGSIGI GFAIPSNLVK RVADEIIKNG SVKHVALGIT ITSDTVEADG
VTRAGAKITK GASGSAVVSG SPADKAGLKE GDTIVAFNGS AVGSNASLLG FVRAAALGDK
ATLTIVRDGK TMDVDVTLDQ QEQSVNGSNR SESSNGSGNS QNNGGNGYGN GSDGSGNSDG
GSDSFGFPFG W
//
