ID R0D1A2_CAUVI Unreviewed; 687 AA.
AC R0D1A2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
DE Flags: Precursor;
GN ORFNames=OR37_01764 {ECO:0000313|EMBL:ENZ82210.1};
OS Caulobacter vibrioides OR37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ82210.1, ECO:0000313|Proteomes:UP000013063};
RN [1] {ECO:0000313|EMBL:ENZ82210.1, ECO:0000313|Proteomes:UP000013063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR37 {ECO:0000313|EMBL:ENZ82210.1,
RC ECO:0000313|Proteomes:UP000013063};
RX PubMed=23792749;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT Tolerant to Heavy Metals.";
RL Genome Announc. 1:0-0(2013).
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:ENZ82210.1}.
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DR EMBL; APMP01000008; ENZ82210.1; -; Genomic_DNA.
DR AlphaFoldDB; R0D1A2; -.
DR STRING; 1292034.OR37_01764; -.
DR PATRIC; fig|1292034.3.peg.1751; -.
DR eggNOG; COG3591; Bacteria.
DR Proteomes; UP000013063; 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..27
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 28..687
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023071901"
SQ SEQUENCE 687 AA; 73729 MW; B9551112EEE8D6BE CRC64;
MVVQRSFSSL AAFGAALLLA ARGEARADEG MWTFDAPPID RIAAATGARL DAAWLDAARA
SAVRLTNGCS GGIVSGQGLV MTNAHCVADC VQTLSGGGED AYLTDARDRE ERCAGLQAEA
LLTITDVTDQ VRASVQGKDG EAYVRAREGA LALAELAACG QDRTLRCQAV SFFRGGQYKV
YKYRRYNDVR LVFAPEAAVA AFGGDPDNFN FPRFAFDVAF LRLYVDEAPA ATPVFLPWRS
TPPAEGEASF VVGNPGSTER QLTVAQLETQ RDLVQPLAQA QRLELRGRLL QFRADDPDRA
RGAAQALAWV ENGVKIGRGR MALLNDRAFM AGKRAEEDAL KARVAADPAL AATAGVAWDR
IADAQDAARD LYPAYRQLEN GPGGSDLFYD ARLLVRAALE RDKPDAERLP EYGDARLPRI
ERRLLDAPPR DLALERIYLE HWLLKTREAL GVDDPRVKAL LGGDSPENLA RALAETRLVD
PAFRAELWAG GRAAVEASDD PLVAFVLRID GMARAARAAY EAKVSGPVDA AAEAIAGARL
ALLGDQIYPD ATFTLRLSYG RVAGWRERGR AVEPFTTFAG FYARASGAPP FVAPPRWLEA
RKALAPDTPF DFVTTNDIVG GNSGSPVLDR RGRVMGAIFD GNSHAIGGAY GYDATANRAV
ALTTAAIGEA LSKVYGRAGL ADELMGR
//
