ID A0A060QIR9_9PROT Unreviewed; 669 AA.
AC A0A060QIR9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase S9, prolyl oligopeptidase {ECO:0000313|EMBL:CDG40588.1};
GN ORFNames=ASAP_2543 {ECO:0000313|EMBL:CDG40588.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG40588.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG40588.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG40588.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG40588.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG40588.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
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:CDG40588.1}.
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DR EMBL; CBLX010000021; CDG40588.1; -; Genomic_DNA.
DR RefSeq; WP_023979919.1; NZ_CBLX010000021.1.
DR AlphaFoldDB; A0A060QIR9; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR Proteomes; UP000027583; Unassembled WGS sequence.
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 Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF07676; PD40; 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;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..669
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001590490"
FT DOMAIN 459..660
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 669 AA; 71376 MW; DB14422B5FEF8487 CRC64;
MSLLSLSRVR LLGTSLLSLG MGSATLGGVT LASAQAQAAP LHFYTAPALS PDGHSLASLD
SMEAVGTAEA APASLVIRTL PDGHATTVAL PCKDCAPSSP SWSPDGTRLA FIIRHKNTQN
REILSVTADG KTVTSLLKFT GSLQDLRYGP KGGLAVLAIA NARRDPGALQ AGAPETGEID
ATEDEQRIAT VEKDGLHWQS PDGLYVYEYD WLPNSTPAFI GTAAPGNGDA HWWSAHLSRF
ADSKEQVLYT HPLSQQIGLP LVSPDGRNVS FVAGLMSDFG FFGGDALQID LSQSKAAPVN
LTRTLKATVT GLNWCQGRLI ASTIAGPMTV MRSIDDKPPL MASADGLLSD GGSEPRLTCA
GDQSVVIRQS FTSPPEIWAG RLGAWQQLTH SNDGQTVPYT ASSVSWVSDG FKVQGWHLVP
RSRPAAMTRN GKVPMITIIH GGPSSAVTPR FLRPTGDAAV LLDAGYDLFL PNPRGSYGQG
EAFTMANRRD FGHGDLRDIQ RGIDALEKTA PIDENRLGVT GYSYGGYMTM WIVTQTNRFK
AAAAGGGIAN WQSYYGQNGI DAWMPPFFGA TVYDDPAIYA HSSPMTFIKQ VRIPTFIYVG
ANDVECPPAQ SLEFYHALRA LGIPTSLVIY PGEGHGMRGH DHASDAQKRM LAWFSRYLNG
SASGKNGAN
//
