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Database: UniProt
Entry: A0A0P0P396_9CAUL
LinkDB: A0A0P0P396_9CAUL
Original site: A0A0P0P396_9CAUL 
ID   A0A0P0P396_9CAUL        Unreviewed;       690 AA.
AC   A0A0P0P396;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Prolyl oligopeptidase {ECO:0000313|EMBL:ALL15038.1};
GN   ORFNames=AQ619_17645 {ECO:0000313|EMBL:ALL15038.1};
OS   Caulobacter henricii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL15038.1, ECO:0000313|Proteomes:UP000056905};
RN   [1] {ECO:0000313|EMBL:ALL15038.1, ECO:0000313|Proteomes:UP000056905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB4 {ECO:0000313|EMBL:ALL15038.1,
RC   ECO:0000313|Proteomes:UP000056905};
RA   Scott D., Ely B.;
RT   "Conservation of the essential genome among Caulobacter and Brevundimonas
RT   species.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP013002; ALL15038.1; -; Genomic_DNA.
DR   RefSeq; WP_062150796.1; NZ_CP013002.1.
DR   AlphaFoldDB; A0A0P0P396; -.
DR   STRING; 69395.AQ619_17645; -.
DR   KEGG; chq:AQ619_17645; -.
DR   OrthoDB; 9801421at2; -.
DR   Proteomes; UP000056905; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR42881:SF13; PROLYL ENDOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000056905};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..690
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006052739"
FT   DOMAIN          27..418
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          486..687
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   690 AA;  74826 MW;  F751FC1C846C4836 CRC64;
     MTLLRTCSAG ALALTLLSHG TALAQDSDPH LALEAVESPD SLAWVNRENA KTLPVLSGDP
     RFAGLQAEAL TILSARDRIA APNFIGTSVF NFWQDATHVR GIWRRTTLAS YKTVSPVWET
     VLDLDALAKA EGKNWIWKGA DCRPKTHDRC LINLSNGGKD AVEVREFDLT TRTFVEGGFR
     LPEGKQNVEW LDADTLILTR DWGPGTTTDS GYGMVIKTLK RGQALSDAVE VFRGQKSDVS
     ARPNVLRDAA GNRVVLIDRA TDFFHTERNV WTDGKVVPLA IPQRAGIAGL LNGRLIVELN
     EDGLGAKAGS IIAVTPDAGL ATSLIFAPSS VQAVDQVTVT DRTVVAAIYD NVRGGVFTFK
     PAGATWTKST LPGLPNASVS LGSHSDEGDQ IFYSVEGFTT PTQLKLADAV SGASETVKAL
     SAQFEGGNLE VEQKVATSKD GTKVPYFLIH PKGHKHDGSN PTLLHAYGGF NLSKLPVYDP
     LIGKLWLEKG GSYAVANIRG GGEFGPAWHE AALKANRQRA FDDYYAVAED MIAKKITSPR
     HLGAYGRSNG GLLMGVALTQ RPDLWNAVVV ESPLLDMIRY TVLPAGASWI GEYGDPAIPA
     ERAWIEAYSP YQNLKPGVKY PLAYITTSTK DDRVHPGHAR KFAARLDDLK VDNLYFENTD
     GGHANGADPK SNARRWALHY TYLSRQLMDH
//
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