ID F7S1D1_9GAMM Unreviewed; 805 AA.
AC F7S1D1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=A28LD_2346 {ECO:0000313|EMBL:EGN74205.1};
OS Idiomarina sp. A28L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN74205.1, ECO:0000313|Proteomes:UP000053031};
RN [1] {ECO:0000313|EMBL:EGN74205.1, ECO:0000313|Proteomes:UP000053031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A28L {ECO:0000313|EMBL:EGN74205.1,
RC ECO:0000313|Proteomes:UP000053031};
RX PubMed=21742887; DOI=10.1128/JB.05648-11;
RA Gupta H.K., Singh A., Sharma R.;
RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT India.";
RL J. Bacteriol. 193:5875-5876(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:EGN74205.1}.
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DR EMBL; AFPO01000028; EGN74205.1; -; Genomic_DNA.
DR AlphaFoldDB; F7S1D1; -.
DR STRING; 1036674.A28LD_2346; -.
DR PATRIC; fig|1036674.4.peg.2324; -.
DR eggNOG; COG3591; Bacteria.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000053031; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053031};
KW Serine protease {ECO:0000256|RuleBase:RU366067}.
FT REGION 586..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 90766 MW; C38115DD1A590813 CRC64;
MSKLHHHGWP KRLWNYLHNG DVKALKFQIK TSFACVFLCT AFFTGAQASE GLWLPEQQPD
WPTQPHASAV LKVGGCTGTF VSPDGLVLTN HHCILDLLQY RSTLENNYLT MGFLAINRNL
ELLAPPDFIV AQTLQRIDVT SQVLQGVNER ITGSARFNLI ANNRNDILRR CEDGINISCR
VVEHYDGLGY LLVRDQNFPQ IKLVWAPPAN VGHFGGLEDN WQWPRHSADL ALLRVYNADG
SAYEPSHWLP LSPAAPADGE PVYVAGFPGT TQRYRLLQEA DMAFAEFYPN LVLYSERWMA
IIETAMQNNP GIALRYIPNL VRQGNRLQNI IGMLGAVEKY DARSLLLEQE QELRDWVAAT
PDNERFTTAI AQTESALEFR QTTLQRQLWW NFFQELQLPL VAQRLYRLAE ESGRAEERRT
RGFQAQQVPA IRSQLISQVR QFAPEVEIKL LVELLVLYQE LPETQRIPFI ETFFELNNSS
SPETITARVE EIYANSKLGD PAVVETLMST SLSDFRRYND PWIQFAVNSA EQRLQWDLQE
RELRGLEQQG RSVLMDAFRR QARSQGKRLP DNANRTFRLS AGYVAAEQEP SALQNEPSAA
EQEPSALQNE PSAAEQEPSA LENEPSAAEQ ELSALEKEPS ALENEPSEHH KAPPARTTLQ
SLLAIAGTEE RYELPFNMHA AVAVHGAGCL AESAEQLTLN FLSTADGTGG SSGSPTVNNR
GELIGLVFDS TTDAILSDWH FDDSRHRMIH ADVRYILWLL RYVYQAHELM AELGFKEDEN
GCSLNDQPII PRPARAGDFH QDPAE
//
