ID A3PD73_PROM0 Unreviewed; 226 AA.
AC A3PD73;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Peptidase E {ECO:0000313|EMBL:ABO17698.1};
DE EC=3.4.11.2 {ECO:0000313|EMBL:ABO17698.1};
GN OrderedLocusNames=P9301_10751 {ECO:0000313|EMBL:ABO17698.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17698.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO17698.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17698.1,
RC ECO:0000313|Proteomes:UP000001430};
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 -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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DR EMBL; CP000576; ABO17698.1; -; Genomic_DNA.
DR RefSeq; WP_011863039.1; NC_009091.1.
DR AlphaFoldDB; A3PD73; -.
DR STRING; 167546.P9301_10751; -.
DR KEGG; pmg:P9301_10751; -.
DR eggNOG; COG3340; Bacteria.
DR HOGENOM; CLU_067063_0_0_3; -.
DR OrthoDB; 9778515at2; -.
DR Proteomes; UP000001430; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR PANTHER; PTHR20842:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ABO17698.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABO17698.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 226 AA; 25330 MW; 4A8264A87F9A3D1D CRC64;
MPSKNIVAIG GGGFGRSLGS LEIEKYIVSL SNKKRPKICF IPTASGDSSL YKLNFYRAFS
KLDCITSHID FFSRTENLEE IVSTQDIIYV GGGNTKSMLA VWKEWNLHKI LRNAYEKGIV
MSGVSAGAIC WFDKGITDSY ANELAIIDCL GIVKGIACPH FDEEKEREPY VFDVIQREII
ETCICIEGNC ALHIKNDFDY SSIDFGNGRN CFRVTKQNNI VKKEIL
//
