ID A0A060QHZ8_9PROT Unreviewed; 696 AA.
AC A0A060QHZ8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=ASAP_2273 {ECO:0000313|EMBL:CDG40318.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG40318.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG40318.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG40318.1,
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:CDG40318.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG40318.1,
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 -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
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:CDG40318.1}.
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DR EMBL; CBLX010000015; CDG40318.1; -; Genomic_DNA.
DR RefSeq; WP_051757708.1; NZ_CBLX010000015.1.
DR AlphaFoldDB; A0A060QHZ8; -.
DR eggNOG; COG3591; Bacteria.
DR Proteomes; UP000027583; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 24..696
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023104263"
SQ SEQUENCE 696 AA; 76053 MW; D7E68E52C3D5A34B CRC64;
MTRARLSLFL SSALFGAVTL ADAARADEGM WTFDHLPNAA LQKTYHFEPD AAWIQHVVQS
SARLAEGCSA SFVSGNGLVM TNHHCANSCL AALSDKDHDY FRNGFYTKDL ADERQCPGME
LDRLDTMKDV SAPVAEATKG KQGAAYSAAL QEVESKLTKD CVGGDDAHWR CDMVSLYHGG
QTALYRYRRY NDVRVVMAPE QGIAFFGGDP DNFDYPRYDI DLSMLRVYEG GKPVNTPFLQ
FDPNGPKADD LVFTSGNPGR TQRGLPAAAL AFQRDVANPA IIAMLSVREG MLWQYSRESA
DHAKQAENTL FGIQNGLKSY SGTQAALQSG DIVSRREKED AALQRWIDAD PARRAAYGQP
FAMVDKAVAL EKDLFTRNLA IGMVFRGFLD DVMTLVEGAH ERAKPDAKRH AGFHDAQLGE
IETSLGAKEP FYPDLETASL ALSLTSLRQV AGADDNLVHL ALGNDAPEDV AARLIKGTKL
SDPAQRLALW KGGLKAIEAS TDPLIVFARK LYPDYASLHD RMRDEVSAPL HKAQGDIARA
RFAQAKAENR LDALYPDATF SPRLSYGTVK GWRKNGTDVA PFTDFAGMYR HATGSEPFAL
PKRWLDAKAN LDLATHLDFV STNDIVGGNS GSPVINREGK AVGLIFDGNL PSLAGDLYYD
ISNNRAVATD TSAIITALRV VYNEKTLADE LTNGHR
//
