ID F7VA38_9PROT Unreviewed; 696 AA.
AC F7VA38;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=ATPR_0237 {ECO:0000313|EMBL:GAA07233.1};
OS Acetobacter tropicalis NBRC 101654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA07233.1, ECO:0000313|Proteomes:UP000004319};
RN [1] {ECO:0000313|EMBL:GAA07233.1, ECO:0000313|Proteomes:UP000004319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA07233.1,
RC ECO:0000313|Proteomes:UP000004319};
RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA Yakushi T., Matsushita K.;
RT "Increased number of Arginine-based salt bridges contributes to the
RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT tropicalis SKU1100.";
RL Biochem. Biophys. Res. Commun. 409:120-124(2011).
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:GAA07233.1}.
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DR EMBL; BABS01000004; GAA07233.1; -; Genomic_DNA.
DR RefSeq; WP_006557247.1; NZ_BABS01000004.1.
DR AlphaFoldDB; F7VA38; -.
DR Proteomes; UP000004319; 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 InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..696
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023160968"
SQ SEQUENCE 696 AA; 76732 MW; 0BC2F3793AA6E40A CRC64;
MAKILRHALV PMALLACAPA IVPYAHADEG MWTMDNLPVK QMQDRYHFTP SKEWIDRVTK
ASARLALGCS ASFVSADGLV MTNHHCANEC LQQLSDKTHN YFQDGYSAKN PAAEQRCPAM
ELNQLDSITD VTDRMQAALK GKEGEAYTKA RQAEESAIEK ECAGADAKTW RCDVISLYHG
GRTALYRYRR YQDVRMVMAP DQNTAFFGGD PDNFNFPRYD LDMAFLRVYE NGKPAKVAAY
LPFDAEGPKD GELVFTSGNP GSTEREVPLA DLEFSRNVTV PFVIDNYSAL DGALWQYSRE
SVAHHQEAQE RIFGIENSLK VYRGRVPVLA DPKLLDAKAK SEASLRDWIN ADEGRKKTYG
DPWAKNAQAL AVKQQIFKPY IMLEGSFGLQ GDLFSYAKLL VRGAYERQKP DAERLTAFHD
GRLPALEAEL GSIAPVYPDL EKTELAFSLT KLRQVLGADD ESVKQVLGKA APDDLAVSLV
NGSKLADPKV RLALWKGGAK AIEASQDPMI VLARKIEPQA RALRKRMDDE VAAPSRQATE
AMAKARFARD GVSSYPDATF TQRLSFGQVK GWDENGKQVA PFTTFAGLYD RATGSDPFKL
SKPWLDAKGR VNLKTPFDFV STNDIIGGNS GSPVIDAQGH AVGLIFDGNI HSLGGDFYYD
ESTNRAVAVD SAAILESLKS VYKNQALADE LVKGHL
//
