ID A0A1H9LDW5_9FIRM Unreviewed; 531 AA.
AC A0A1H9LDW5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605};
GN ORFNames=SAMN02910369_03043 {ECO:0000313|EMBL:SER09439.1};
OS Lachnospiraceae bacterium NE2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520823 {ECO:0000313|EMBL:SER09439.1, ECO:0000313|Proteomes:UP000199680};
RN [1] {ECO:0000313|EMBL:SER09439.1, ECO:0000313|Proteomes:UP000199680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE2001 {ECO:0000313|EMBL:SER09439.1,
RC ECO:0000313|Proteomes:UP000199680};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; FOEK01000039; SER09439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LDW5; -.
DR STRING; 1520823.SAMN02910369_03043; -.
DR OrthoDB; 53505at2; -.
DR Proteomes; UP000199680; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..514
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 531 AA; 60408 MW; 6C3E08F7BA8AAF15 CRC64;
MHFGFSYVGL IFLLMLFIPN GIWAKNPPKD YEEFSKNENK VLLIFERIGE VLVSTLVLIF
ADCNVRIHSL WIGWLVIAFI LMILYECYWV KYFKSEKTMA DMYSSFAGFP VAGASLPVIA
VLFLGIYACN IFIILASIIL GIGHIGIHLN HRKEAMGEET EKNSEKTYEN KVKNSKKKKI
LKIIKIIVLV PIVLYVAICI VLIGIRNINF FTSIIDTREG VDEATYVELN GQQQYITIRG
RKKDNPVILY LHGGPGSPDS MMTYNFTNKL IDEYTVVCWD QRGCGRTYLK NDDKENETVT
ADQAIEDIDA LVDYLSNRFN QEKIVIIGHS YGSVIGSRYA YEHPEKTAAF IGVGQFVSFE
TSAECEYLDA LEKAQAAGDD TTELSNAYEN YVREKTLDAA SEITKYAAKY HKAPRSKNTI
LTALVSPTFE TDDVLWYTKV LNYEQFMKYN ENLIDYLLEV NLRETQESYA VPVFFISGSC
DWNCAVTDMT DYAEMVSGKY DIIEGCGHYV HNDDPDAFAQ IVKEDLESIE Y
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