ID   B2ITT3_NOSP7            Unreviewed;       312 AA.
AC   B2ITT3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   04-NOV-2026, entry version 87.
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   OrderedLocusNames=Npun_F5930 {ECO:0000313|EMBL:ACC84221.1};
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
OC   Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC84221.1, ECO:0000313|Proteomes:UP000001191};
RN   [1] {ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACC84221.1, ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX   PubMed=23463784; DOI=10.1104/pp.112.213116;
RA   Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT   "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT   Cyanobacterium-Plant Symbiosis.";
RL   Plant Physiol. 161:1984-1992(2013).
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; CP001037; ACC84221.1; -; Genomic_DNA.
DR   RefSeq; WP_012412164.1; NC_010628.1.
DR   STRING; 63737.Npun_F5930; -.
DR   ESTHER; nosp7-b2itt3; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; ACC84221; ACC84221; Npun_F5930.
DR   KEGG; npu:Npun_F5930; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_043739_2_2_3; -.
DR   OMA; AACRYWA; -.
DR   OrthoDB; 9775557at2; -.
DR   PhylomeDB; B2ITT3; -.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
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.
DR   NCBIfam; TIGR01249; pro_imino_pep_1; 1.
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:InterPro.
DR   Proteomes; UP000001191; Chromosome.
DR   AlphaFoldDB; B2ITT3; -.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|PIRNR:PIRNR006431};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR006431};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006431};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR006431};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001191}.
FT   DOMAIN          36..296
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT   ACT_SITE        294
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ   SEQUENCE   312 AA;  35806 MW;  A3D61A67EDD6370D CRC64;
     MRELYPAIEP YREGSLQVSD LHTIHFEESG NPQGQPMILL HGGPGGGCPP FYRQYFHPEK
     WRIVMFDQRG CGQSKPHAEL RENTTWDLVS DIEKLRQHLE IEKWAVFGGS WGSTLSLAYS
     QTHPSCCTAL ILRGIFMLRQ KELRWFYQEG ASYIFPDAWE AYVEPIAIAE RDDMIAAYYK
     RLTSPDLEIQ LAAARAWSIW EASTSRLFLD PELMQKFGES EFASAFARIE CHYFMNKGFL
     ETEDQLLLNV DRIRHIPAVI VQGRYDVVCP MISAWELHRA WPEAEFIVVS DAGHSMSEPG
     IRSALIEATD NI
//