ID A0A086BP49_9BIFI Unreviewed; 516 AA.
AC A0A086BP49;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
GN ORFNames=BBOMB_0019 {ECO:0000313|EMBL:KFF30713.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF30713.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF30713.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF30713.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|PIRNR:PIRNR005700}.
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:KFF30713.1}.
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DR EMBL; ATLK01000001; KFF30713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086BP49; -.
DR STRING; 1341695.BBOMB_0019; -.
DR eggNOG; COG3579; Bacteria.
DR Proteomes; UP000028730; Unassembled WGS sequence.
DR GO; GO:0070005; F:cysteine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00585; Peptidase_C1B; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR004134; Peptidase_C1B.
DR PANTHER; PTHR10363; BLEOMYCIN HYDROLASE; 1.
DR PANTHER; PTHR10363:SF2; BLEOMYCIN HYDROLASE; 1.
DR Pfam; PF03051; Peptidase_C1_2; 2.
DR PIRSF; PIRSF005700; PepC; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700,
KW ECO:0000313|EMBL:KFF30713.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005700};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005700};
KW Reference proteome {ECO:0000313|Proteomes:UP000028730};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 457
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 516 AA; 58854 MW; BB33661009B9C041 CRC64;
MDTNVHTPPI MKGPSNMSKA SKTVKKPATR AGKENEKAIS SRAIDEYSKR FNSERANRVA
ANASTSLGLI KAATSYQGVR SLPKDFSVDL KQTGITNQKQ SGRCWMFAAL NTLSFEVMHK
WNLDDFEFSE SYLFFWDKIE KSNTYLENVL ATLDEDTDSR IFTIINYEPA DDGGWWQMFV
NLVNKYGLMP KSAFPESANS GNSDDFTMYL NVKLREFASQ LREEHQAGAS LDKLRELKLN
DMETVYRICA ISLGEPPKKF DFFARTKEDD KKEDCKDEKT KSDGKTKNVS KDAKDSKESR
IDDRPQIREY GITPQEFYAK YVPVDVNDYV TLCNNPMKSR PFNRRYQLKF STNVAETGPL
EFVNVDMDTI HKAALDQLQA GHPLWFACDC DQYALLRGKE GIFDPGAVRV DELFGTEFTF
DKAHALQYGV SSANHAMTFT GVNIDEDGQA DRWKVENSWG KDVGEDGYYV ASDEWFRRYV
NELIVRKEFL PEPVLDALQS EPLTLEPWQS LSSICR
//
