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Database: UniProt
Entry: A3D659_SHEB5
LinkDB: A3D659_SHEB5
Original site: A3D659_SHEB5 
ID   A3D659_SHEB5            Unreviewed;       429 AA.
AC   A3D659;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Prolyl aminopeptidase 2. Serine peptidase. MEROPS family S33 {ECO:0000313|EMBL:ABN62222.1};
GN   OrderedLocusNames=Sbal_2735 {ECO:0000313|EMBL:ABN62222.1};
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN62222.1, ECO:0000313|Proteomes:UP000001557};
RN   [1] {ECO:0000313|EMBL:ABN62222.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; CP000563; ABN62222.1; -; Genomic_DNA.
DR   RefSeq; WP_011847172.1; NC_009052.1.
DR   AlphaFoldDB; A3D659; -.
DR   STRING; 325240.Sbal_2735; -.
DR   ESTHER; sheb5-a3d659; Proline_iminopeptidase.
DR   KEGG; sbl:Sbal_2735; -.
DR   HOGENOM; CLU_024518_2_0_6; -.
DR   OrthoDB; 9796770at2; -.
DR   Proteomes; UP000001557; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:ABN62222.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:ABN62222.1}.
FT   DOMAIN          50..217
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   429 AA;  48774 MW;  9872C0A3B0092147 CRC64;
     MKPDIILAGV LAKKHTFTLP LNYQNPIAEQ IQVFARELCS PENKDKKLPY IVFFQGGPGF
     AAMRPASNSG WIRRALKEYR VLLLDQRGTG LSTPINYQSL QHLEPTAQAD YLSHFRADNI
     IRDAETIRAQ LCPADKWAIL GQSFGGFCVL HYLSAAPQGV SEAYITGGIP SLTRSADDVY
     LATYQRVLAK NKQFFQRFHD AQHLVTRLAK HLLENEVYLA TGERLTVEML QLLGINIGME
     QGPESVYYLL EQALINTASG TVVNPLFLNH FGQMLDYNTN PIFALLHEAI YCQHSASQWA
     AHRVRQQFPA FNYQQGKPFL FTGEMIYPWM FDQFSHLVPL KAAAEILAHK SDWPALYNLE
     QLAQNRVPVA TAIYSEDMFV EMQYSLETAQ QVGRLKYWLT SEYEHNGIRM DGEHILDKLI
     SLNRGDTLR
//
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