ID D9Q9F0_CORP2 Unreviewed; 339 AA.
AC D9Q9F0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN Name=pip {ECO:0000313|EMBL:ADL10176.1};
GN ORFNames=CPC231_03495 {ECO:0000313|EMBL:ADL10176.1};
OS Corynebacterium pseudotuberculosis (strain C231).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10176.1, ECO:0000313|Proteomes:UP000000276};
RN [1] {ECO:0000313|EMBL:ADL10176.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL10176.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21037006; DOI=.1128/JB.01211-10;
RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT strain isolated from a cow in Israel with bovine mastitis.";
RL J. Bacteriol. 193:323-324(2011).
RN [2] {ECO:0000313|EMBL:ADL10176.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL10176.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT "Evidence for reductive genome evolution and lateral acquisition of
RT virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL PLoS ONE 6:E18551-E18551(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; CP001829; ADL10176.1; -; Genomic_DNA.
DR RefSeq; WP_013241551.1; NC_017301.2.
DR AlphaFoldDB; D9Q9F0; -.
DR STRING; 681645.CpC231_0694; -.
DR ESTHER; corp1-d9q7e0; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR GeneID; 69460091; -.
DR KEGG; cpq:CPC231_03495; -.
DR PATRIC; fig|681645.3.peg.724; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_043739_2_2_11; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000000276; 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; 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:UP000000276}.
FT DOMAIN 37..318
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 339 AA; 37910 MW; 43865670B08DFD46 CRC64;
MKTLYPVADP IAQSYIEREG QRIAYTEYGN PQGIPAVFIH GGPGGGTTKE NAGFFDQDKY
RVILIDQRGC GKSTPHIADP DTDLESALAA NTTPKLVEDI EAIRQQLGID KWLVFGGSWG
STLSLKYTQT HPDRVLAVVL RGIFMLRKTE LDWFYNGGAA HLFPDKWERY LSVIPEDKKP
AAGDLSGATH LDGVDLIAEY HKLLHSQDRA VALEAARAWS VWEGSTSFLE IRDTHDHEDE
RFALAFARIE NHYFMHQGFM RDGELLEPAN IERIRNIPAV IVQGRYDVVC PPVTAWNLHR
AWPEAEFHFS PTSGHAASEK ENVAALVAAT DRFAEELSK
//
