PDUV_CITFR
ID PDUV_CITFR Reviewed; 150 AA.
AC B1VB80;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Propanediol utilization protein PduV;
GN Name=pduV {ECO:0000303|PubMed:18332146};
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT "Biochemical and Structural Insights into Bacterial Organelle Form and
RT Biogenesis.";
RL J. Biol. Chem. 283:14366-14375(2008).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RX PubMed=20417607; DOI=10.1016/j.molcel.2010.04.008;
RA Parsons J.B., Frank S., Bhella D., Liang M., Prentice M.B., Mulvihill D.P.,
RA Warren M.J.;
RT "Synthesis of empty bacterial microcompartments, directed organelle protein
RT incorporation, and evidence of filament-associated organelle movement.";
RL Mol. Cell 38:305-315(2010).
CC -!- FUNCTION: May play a role in the spatial distribution of the bacterial
CC microcompartment (BMC) dedicated to 1,2-PD degradation, perhaps being
CC involved in cytoskeleton dynamics; might bind GTP (Probable). This
CC subunit is directly targeted to the BMC (PubMed:20417607).
CC {ECO:0000269|PubMed:20417607, ECO:0000305|PubMed:20417607}.
CC -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC appearance of bacterial microcompartments (BMC) in its cytoplasm.
CC {ECO:0000269|PubMed:18332146}.
CC -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC volatile reaction intermediates thus enhancing pathway flux and keeps
CC the level of toxic, mutagenic propionaldehyde low.
CC {ECO:0000305|PubMed:20417607}.
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:18332146}.
CC -!- SUBUNIT: Interacts with PduU, probably via the PduU beta-barrel which
CC is predicted by modeling to be on the exterior of the BMC.
CC {ECO:0000250|UniProtKB:Q9XDM6}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:20417607}. Note=Probably found on the exterior of
CC the BMC. {ECO:0000305|PubMed:20417607}.
CC -!- DOMAIN: The N-terminus is required for targeting to the BMC; 42
CC residues target GFP to the BMC, although 98 residues give better
CC targeting. {ECO:0000269|PubMed:20417607}.
CC -!- BIOTECHNOLOGY: Can be used to target proteins to the BMC (tested with
CC GFP). {ECO:0000269|PubMed:20417607}.
CC -!- SIMILARITY: Belongs to the EutP/PduV family.
CC {ECO:0000255|PIRNR:PIRNR036409}.
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DR EMBL; AM498294; CAM57301.1; -; Genomic_DNA.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0006576; P:cellular biogenic amine metabolic process; IEA:InterPro.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012381; EutP_PduV.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR40453; PTHR40453; 1.
DR Pfam; PF10662; PduV-EutP; 1.
DR PIRSF; PIRSF036409; EutP_PduV; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02528; EutP; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; GTP-binding; Nucleotide-binding.
FT CHAIN 1..150
FT /note="Propanediol utilization protein PduV"
FT /id="PRO_0000454285"
FT REGION 1..42
FT /note="Targets protein to the BMC"
FT /evidence="ECO:0000269|PubMed:20417607"
FT BINDING 8..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:20417607"
SQ SEQUENCE 150 AA; 16332 MW; 8DC6D70EFBCBAF85 CRC64;
MKRIMLIGPS QCGKTSLTQC MRGEALHYQK TQAIVWSPTT IDTPGEYLEN RCLYSALLAS
ACEADIIALV LNADAPWSPF SPGFTGPMNR PVIGLVTKAD LASPQRISLV ESWLVQAGAQ
KVFFTSALEN TGVDEMFIFL NAKESSCLTK