ID Q7TUE6_PROMP Unreviewed; 315 AA.
AC Q7TUE6;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=PMM0356 {ECO:0000313|EMBL:CAE18815.1};
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE18815.1, ECO:0000313|Proteomes:UP000001026};
RN [1] {ECO:0000313|EMBL:CAE18815.1, ECO:0000313|Proteomes:UP000001026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4
RC {ECO:0000313|Proteomes:UP000001026};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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; BX548174; CAE18815.1; -; Genomic_DNA.
DR RefSeq; WP_011131993.1; NC_005072.1.
DR AlphaFoldDB; Q7TUE6; -.
DR STRING; 59919.PMM0356; -.
DR ESTHER; proma-PMM0356; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR KEGG; pmm:PMM0356; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_043739_2_2_3; -.
DR OrthoDB; 9775557at2; -.
DR Proteomes; UP000001026; 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}.
FT DOMAIN 38..297
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 111
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 315 AA; 36454 MW; D01CA6A5C078C2C5 CRC64;
MKENLFPSIE PREKGFLQVS KIHSIYWERS GNPKGKKILV IHGGPGGGSQ PRYRRYFNPE
KFDIVQFDQR GCGYSRPFSE LRENTTGDLV NDIEKLRVNL KIDYWHLFGG SWGSTLALIY
AIKNPSRVLS MTLRGIFLCR KFELLWFYQY GASEIFPEEF EKYIAVIPKD ERVDLIVSFY
KYLTSPDIEL RSKAAAAWTN WELSTSHLIK RDIDVGKSKI NSFSDAFARI ECHYFINKIF
LEENFILKNA KIIESIPTKI IQGRYDVVCP VRSAWDLSRK LINSELIIVD DAGHSMSEKG
ITLKLLDSVE RLESF
//
