ID   Q0VM92_ALCBS            Unreviewed;       307 AA.
AC   Q0VM92;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 109.
DE   RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR006431};
DE            Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE            EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR006431};
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605, ECO:0000256|PIRNR:PIRNR006431};
GN   Name=pip {ECO:0000313|EMBL:CAL17706.1};
GN   OrderedLocusNames=ABO_2257 {ECO:0000313|EMBL:CAL17706.1};
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Oceanospirillales; Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL17706.1, ECO:0000313|Proteomes:UP000008871};
RN   [1] {ECO:0000313|EMBL:CAL17706.1, ECO:0000313|Proteomes:UP000008871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2
RC   {ECO:0000313|Proteomes:UP000008871};
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL17706.1; -; Genomic_DNA.
DR   RefSeq; WP_011589532.1; NC_008260.1.
DR   AlphaFoldDB; Q0VM92; -.
DR   STRING; 393595.ABO_2257; -.
DR   ESTHER; alcbs-q0vm92; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   KEGG; abo:ABO_2257; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_043739_2_2_6; -.
DR   OrthoDB; 9796770at2; -.
DR   Proteomes; UP000008871; 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:InterPro.
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   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|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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR006431};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008871};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        103..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..286
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT   ACT_SITE        283
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ   SEQUENCE   307 AA;  34124 MW;  CA3D9A3FC827EA8F CRC64;
     MALFPYLDAN RQFYLPVGEG HQLYVEESGN PQGSPVVVLH GGPGGGCSPA LRRFFDPQKF
     RMILFDQRGS GQSRPLGSID NNTLSHLLLD LEKIRQALHI ERWMVFGGSW GATLALAYLA
     AFPQYITAMV LRGIFLCRER DLDWLYTSKG AARLFPEAWQ ALEQQAPPGS GHLLERYYQG
     LQGDDAHRYA RAWCNWESTL ALMPTQPPGA GSDGELCMAR QETHYFLAGG FIERPLLEVC
     AGSQVPVEIV HGRRDFVCPP EQALALHQVL PNSELNWVDR GGHSSMDPGV AQALVNAVTR
     LDRRAKQ
//