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Database: UniProt
Entry: A0A1A9LDB2_9FLAO
LinkDB: A0A1A9LDB2_9FLAO
Original site: A0A1A9LDB2_9FLAO 
ID   A0A1A9LDB2_9FLAO        Unreviewed;       372 AA.
AC   A0A1A9LDB2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Aminopeptidase {ECO:0000256|PIRNR:PIRNR005700};
GN   ORFNames=A7A78_12320 {ECO:0000313|EMBL:OAD91359.1};
OS   Aequorivita soesokkakensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=1385699 {ECO:0000313|EMBL:OAD91359.1, ECO:0000313|Proteomes:UP000077552};
RN   [1] {ECO:0000313|EMBL:OAD91359.1, ECO:0000313|Proteomes:UP000077552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSSK-12 {ECO:0000313|EMBL:OAD91359.1,
RC   ECO:0000313|Proteomes:UP000077552};
RA   Thevarajoo S., Selvaratnam C., Goh K.M., Chan K.-G., Chong C.S.;
RT   "Genome sequencing of Vitellibacter soesokkakensis RSSK-12.";
RL   Submitted (MAY-2016) 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:OAD91359.1}.
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DR   EMBL; LXIE01000014; OAD91359.1; -; Genomic_DNA.
DR   RefSeq; WP_068761916.1; NZ_LXIE01000014.1.
DR   AlphaFoldDB; A0A1A9LDB2; -.
DR   STRING; 1385699.A7A78_12320; -.
DR   OrthoDB; 9814054at2; -.
DR   Proteomes; UP000077552; 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; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR004134; Peptidase_C1B.
DR   PANTHER; PTHR10363; BLEOMYCIN HYDROLASE; 1.
DR   PANTHER; PTHR10363:SF2; BLEOMYCIN HYDROLASE; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   Pfam; PF03051; Peptidase_C1_2; 1.
DR   PIRSF; PIRSF005700; PepC; 2.
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:OAD91359.1};
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..372
FT                   /note="Aminopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008392093"
FT   DOMAIN          32..114
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00112"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005700-1"
SQ   SEQUENCE   372 AA;  42082 MW;  ACC1E490F0A0C9E1 CRC64;
     MKHFLSFFAI LFTITLTAQQ PYKFTTITDL EATPVISQGI TGTCWSFSST SFLESEIIRL
     TGKKIDLSEM YQVRNTYPLK AENYIMRQGR AQFGEGGLAH DVMNSVERNG LVPEEAFSGL
     FVGETVYNHA EMVAVLEAML KTYVDNPGRK LSKKWRSAIE GVLDAYIGKN LTNFTFEGKQ
     YTPQTFLAMT KIQPADYVNL TSFTQAPFYS QFILNIPDNW SNGSFYNVPL DEMMATIDNA
     LEKGFTVELD CDVSEKTFSS KDGVAVIPEN AENNVKALQG IYPEKKITQE YRQEEFENYD
     TTDDHLMHIT GILQDQNGTK YYKVKNSWGT DETRVANGGY IYFSEAYMRL KAISVTVHKD
     ALPKNTATKL NL
//
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