ID A3VLH4_9RHOB Unreviewed; 314 AA.
AC A3VLH4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 03-MAY-2023, entry version 73.
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 ORFNames=RB2654_21878 {ECO:0000313|EMBL:EAQ10862.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ10862.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ10862.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ10862.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ10862.1}.
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DR EMBL; AAMT01000023; EAQ10862.1; -; Genomic_DNA.
DR RefSeq; WP_008335762.1; NZ_VNHV01000007.1.
DR AlphaFoldDB; A3VLH4; -.
DR STRING; 314271.RB2654_21878; -.
DR ESTHER; 9rhob-a3vlh4; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_043739_2_2_5; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000002931; Unassembled WGS sequence.
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 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; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW ECO:0000313|EMBL:EAQ10862.1}; Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431};
KW Protease {ECO:0000256|PIRNR:PIRNR006431};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931}.
FT DOMAIN 31..289
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 314 AA; 34947 MW; 690FA093EC7A6F03 CRC64;
MKELTRDNLA VGDGHEIHVR SYGNPGGIPA LFLHGGPGSG VQESQLGIFD PSRFHVIAFD
QRGAGLSRFD DRFHANTTPH LVADIERIRE RFGIERWMVV GGSWGATLAL AYATAHADRI
GAMVLRAVFL GTRHELERAF LSSLPRFYPQ LYADFVGLLP EDDRSRVLDA YWDRILDADP
AVHRPFSIAW HDTERVLSVL SPDVPCLSED LSARGDRPLP RTPFMEAHYF HNDCFLDAPL
IEQVHRLNGL PGILIQGRYD LLCPPETSYA LASRWTGSSV RVVSPAGHSM EDQSIRSALT
AAITEMARLM NGRL
//