ID A0A1F3EAE5_9BACT Unreviewed; 399 AA.
AC A0A1F3EAE5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
GN ORFNames=A2X13_06330 {ECO:0000313|EMBL:OFX51566.1};
OS Bacteroidetes bacterium GWC2_33_15.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797324 {ECO:0000313|EMBL:OFX51566.1, ECO:0000313|Proteomes:UP000177978};
RN [1] {ECO:0000313|EMBL:OFX51566.1, ECO:0000313|Proteomes:UP000177978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFX51566.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MENN01000010; OFX51566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3EAE5; -.
DR Proteomes; UP000177978; Unassembled WGS sequence.
DR GO; GO:0070005; F:cysteine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 1.
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:OFX51566.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005700};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005700};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR005700}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..399
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009488392"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 335
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT ACT_SITE 356
FT /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ SEQUENCE 399 AA; 45513 MW; 9FD7A2EC7F2CC5C4 CRC64;
MNKKLIAYIA ILLLANGTLS AQENTGKKSA YQFTVVKEIR TTPVKDQNRS GTCWSFSTIS
FLESEMLRMG KPEVNLSEAW VVRHSYSDKA KLYVRWQGSL NFAGGGGFHD VTNCIKKYGI
VPEEVYAGLN YGTEKFVHNE MDAVLKAYMD QVIKNPNKEL STAWHNGLEG ILDAYLGEKV
EKFTYNGKEY TPKTFAAEYV GINPDDYIEV TSFTHHPYYT KFILELPDNW SFDEVYNVTL
DDFIQIIDNS IEMGYTVAWG GDVSEKGFSW KNGVAIVPDI KYEETSGSDK ERLTGLTAKE
KDEILYSFEK QLKELEITPE LRQKEFDNYN TTDDHGMHIV GIAKDQNGNK FYKVKNSWDI
DNPYNGYIFM SEAFIKFKAT DIMIHKNGIP KEIAKKLGL
//
