PIP_MYCGE
ID PIP_MYCGE Reviewed; 308 AA.
AC P47266;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative proline iminopeptidase;
DE Short=PIP;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase;
DE Short=PAP;
GN Name=pip; OrderedLocusNames=MG020;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-308.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
CC -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline
CC residues from peptides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR EMBL; L43967; AAC71236.1; -; Genomic_DNA.
DR EMBL; U02229; AAA03381.1; -; Genomic_DNA.
DR PIR; B64202; B64202.
DR RefSeq; WP_009885920.1; NZ_AAGX01000010.1.
DR AlphaFoldDB; P47266; -.
DR SMR; P47266; -.
DR STRING; 243273.MG_020; -.
DR ESTHER; mycge-pip; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR EnsemblBacteria; AAC71236; AAC71236; MG_020.
DR KEGG; mge:MG_020; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_043739_2_2_14; -.
DR OMA; FYQDGAS; -.
DR OrthoDB; 665798at2; -.
DR BioCyc; MGEN243273:G1GJ2-20-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005944; Pro_iminopeptidase.
DR PANTHER; PTHR43722; PTHR43722; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF006431; Pept_S33; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..308
FT /note="Putative proline iminopeptidase"
FT /id="PRO_0000080839"
FT DOMAIN 30..290
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 261
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 308 AA; 35289 MW; 65087048D205EEF3 CRC64;
MNTKLNVKGY LNVGDNHQLY YWTQGNPNGK PVLYIHGGPG SGTDEGCLKY FDLETTWIIL
LDQRGCGKSK TNDIFYENNT DKLVSDFEIL RQKLNIKNWT LFGGSWGSAL ALVYAIKHPQ
VVDKIFLRAL FLAREKDWSE ALMGLGKMFY PYEHQRFMDS IPKAYQNSYE QIVNYCYDQF
QNGDESTKEK LAKAWVDWES TLLSPINKIH STATDFKLVE KLALLECHYA VNKSFLDENF
ILDNISVLKN KSIYLAHGRF DLICPLYQPL ALKQAFPELQ LYVTNNAGHS GSDANNLATI
KHLLKTYL