ID   A2C6E9_PROM3            Unreviewed;       652 AA.
AC   A2C6E9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Esterase/lipase/thioesterase family active site {ECO:0000313|EMBL:ABM77059.1};
GN   Name=dap2 {ECO:0000313|EMBL:ABM77059.1};
GN   OrderedLocusNames=P9303_03061 {ECO:0000313|EMBL:ABM77059.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM77059.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM77059.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM77059.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM77059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C6E9; -.
DR   STRING; 59922.P9303_03061; -.
DR   MEROPS; S09.074; -.
DR   KEGG; pmf:P9303_03061; -.
DR   HOGENOM; CLU_012236_1_0_3; -.
DR   BioCyc; PMAR59922:G1G80-292-MONOMER; -.
DR   Proteomes; UP000002274; Chromosome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR43056:SF5; ACYL-PEPTIDE HYDROLASE; 1.
DR   PANTHER; PTHR43056; PEPTIDASE S9 PROLYL OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          446..651
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  72431 MW;  19E08A719656EF5F CRC64;
     MESTSHHQRN PKQTTQPLSA RRALGQTPTL KEPRLIDDWV LWLEQRPQEH GRTTALIRPW
     GQSDHPPQEL TPAPANLRSR IHDYGGGVLA TACQDNQLLM AWIDDADGCL WFQRWQGLNQ
     ATKGKKALSP LKPPLRLSKP NDAQLADGLI DLPRQRWLGI MEADKRDWLV TFSLNHENQA
     ATVLHRPADF AGYAILSPNG DQLAWVEWQQ PAMPWEASQL WWASLDPAGL IQSSACLAGS
     KPLDHKQTSV FQPLWLPNGE LVVSEDSSGW WNLMVAKLTT DPTVQPTWRR PWPLSAETGM
     PQWVYGMSSS AWDGEQILTA VCEQGSWRLS RLADDGQIST INQPFDDLNG LQAQEGRAVA
     IASNATTSPG LLELNLNCGS WKHTPANEPL LNADAISVAE PIWFEGCHGQ ATHAWYYPPI
     NGSKGPAPLL VKSHSGPTSM ANHGLSLSIQ FWTCRGWGVV DVNYGGSTGF GRAYRERLRG
     GWGETDVTDC AQAALALVKC NKANPTQIAI EGGSAGGFTT LACLCFTDVF RAAACRYAVS
     DLTAMAEDTH RFEARYLDHL VGRWPDQRQL YENRSPLLHA NKIQCPVIFF QGLQDKVVPP
     DQTERMANAL KENGIPVELH IFEQEGHGFR DSAVKIKVLE ATEQFFRRHL KL
//