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Database: UniProt
Entry: A0A2P8C8M1_9BACT
LinkDB: A0A2P8C8M1_9BACT
Original site: A0A2P8C8M1_9BACT 
ID   A0A2P8C8M1_9BACT        Unreviewed;       403 AA.
AC   A0A2P8C8M1;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
GN   ORFNames=CLV93_11082 {ECO:0000313|EMBL:PSK81298.1};
OS   Prolixibacter denitrificans.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Prolixibacter.
OX   NCBI_TaxID=1541063 {ECO:0000313|EMBL:PSK81298.1, ECO:0000313|Proteomes:UP000240621};
RN   [1] {ECO:0000313|EMBL:PSK81298.1, ECO:0000313|Proteomes:UP000240621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27267 {ECO:0000313|EMBL:PSK81298.1,
RC   ECO:0000313|Proteomes:UP000240621};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSK81298.1}.
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DR   EMBL; PYGC01000010; PSK81298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8C8M1; -.
DR   Proteomes; UP000240621; 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; 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   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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..403
FT                   /note="Aminopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015135930"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        339
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ   SEQUENCE   403 AA;  46265 MW;  53C34EF28C516DEF CRC64;
     MNRFKFFMLL AGLLAFTWNV SAQDKEKSSK EEGYHFTTVK ELPHTSVKDQ YRSGTCWAFS
     GLSFLESEML RMGKPKVNLS EMFVVYHCYI DKAIKTVRLH GNLNFGPGGA FHDVTYVLKN
     YGIVPEDVYT GLNYGEKKHV HGEMDDVLKG IVDAVIENKN KKLSTAWEES VTGTLDAYLG
     DLPTKFEYKG KEYTPKTFAN EYCGLNPDDY VEITSFTHHP FYSKFKLEVP DNWEWDEVYN
     VPLDEMMKII DNSLNSGYTV AWAADVSEKG FSTSKKGVAV VPDADVKDMT NTELSKWEKL
     TAKEKNEQLY KLDKPGKEKH ITQEMRQEAF DDWQTTDDHG MHIIGLAKDQ NGTMYYKVKN
     SWGDYNAWDG YFYASKPYVR YKTTCIMVNK NAIPKAIREK LGL
//
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