ID D9QK18_BRESC Unreviewed; 324 AA.
AC D9QK18;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR006431};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR006431};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN OrderedLocusNames=Bresu_2293 {ECO:0000313|EMBL:ADL01603.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL01603.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585,
CC ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006431}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR006431,
CC ECO:0000256|RuleBase:RU003421}.
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DR EMBL; CP002102; ADL01603.1; -; Genomic_DNA.
DR RefSeq; WP_013269704.1; NC_014375.1.
DR AlphaFoldDB; D9QK18; -.
DR STRING; 633149.Bresu_2293; -.
DR ESTHER; bresc-d9qk18; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR KEGG; bsb:Bresu_2293; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_043739_2_2_5; -.
DR InParanoid; D9QK18; -.
DR OrthoDB; 9796770at2; -.
DR BioCyc; BSUB633149:G1GM8-2292-MONOMER; -.
DR Proteomes; UP000002696; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005944; Pro_iminopeptidase.
DR NCBIfam; TIGR01249; pro_imino_pep_1; 1.
DR PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF006431; Pept_S33; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW ECO:0000256|RuleBase:RU003421}; Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Protease {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Reference proteome {ECO:0000313|Proteomes:UP000002696}.
FT DOMAIN 44..305
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 303
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 324 AA; 36584 MW; 60946E23C98DC9E9 CRC64;
MSFPVTETPR RELYPEIEPF ASGWMQTGSA HEIYFEEVGN PQGKPVLVLH GGPGGAINAG
MRRYFDPSIY RIVLFDQRGC GKSRPNASLE DNTTWTLIED IERLRERCGI ESWAVFGGSW
GSTLSLAYAI THPERVTALI LRGIFLLTKK ELLWFYQDGA SMIFPDAWER FVAPIPEDER
HDLMGAYYKR LTGDDRAEQE RCAIAWSSWE GETVSVEGPS ARPDKFAEPE FAIAFARIEC
WYFMNGGFFP EEHWLLKNIG RIRHIPTWIA QGRFDVVTPI SGAWSLHRAF PEAKLDIVPD
AGHASSEPGI IDSLIRGTDW AATV
//
