ID   PDUV_SALTY              Reviewed;         150 AA.
AC   Q9XDM6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Propanediol utilization protein PduV;
GN   Name=pduV {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2056;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION.
RC   STRAIN=LT2;
RX   PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA   Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT   "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT   typhimurium LT2 includes genes necessary for formation of polyhedral
RT   organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT   degradation.";
RL   J. Bacteriol. 181:5967-5975(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   BACTERIAL MICROCOMPARTMENT ABUNDANCE.
RC   STRAIN=LT2;
RX   PubMed=12923081; DOI=10.1128/jb.185.17.5086-5095.2003;
RA   Havemann G.D., Bobik T.A.;
RT   "Protein content of polyhedral organelles involved in coenzyme B12-
RT   dependent degradation of 1,2-propanediol in Salmonella enterica serovar
RT   Typhimurium LT2.";
RL   J. Bacteriol. 185:5086-5095(2003).
RN   [4]
RP   INTERACTION WITH PDUU, AND SUBCELLULAR LOCATION.
RC   STRAIN=LT2;
RX   PubMed=25646976; DOI=10.1371/journal.pcbi.1004067;
RA   Jorda J., Liu Y., Bobik T.A., Yeates T.O.;
RT   "Exploring bacterial organelle interactomes: a model of the protein-protein
RT   interaction network in the Pdu microcompartment.";
RL   PLoS Comput. Biol. 11:e1004067-e1004067(2015).
RN   [5]
RP   SYSTEM-MODELING, AND FUNCTION.
RC   STRAIN=LT2;
RX   PubMed=28475631; DOI=10.1371/journal.pcbi.1005525;
RA   Jakobson C.M., Tullman-Ercek D., Slininger M.F., Mangan N.M.;
RT   "A systems-level model reveals that 1,2-Propanediol utilization
RT   microcompartments enhance pathway flux through intermediate
RT   sequestration.";
RL   PLoS Comput. Biol. 13:e1005525-e1005525(2017).
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. This subunit is directly targeted to
CC       the BMC (By similarity). Might bind GTP (Probable).
CC       {ECO:0000250|UniProtKB:B1VB80, ECO:0000305|PubMed:25646976}.
CC   -!- FUNCTION: The 1,2-propanediol (1,2-PD) degradation bacterial
CC       microcompartment (BMC) concentrates low levels of 1,2-PD catabolic
CC       enzymes, concentrates volatile reaction intermediates thus enhancing
CC       pathway flux and keeps the level of toxic, mutagenic propionaldehyde
CC       low. {ECO:0000305|PubMed:28475631}.
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000305|PubMed:10498708}.
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:0000269|PubMed:25646976}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000305|PubMed:25646976}. Note=Probably found on the exterior of
CC       the BMC. {ECO:0000305|PubMed:25646976}.
CC   -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC       medium. {ECO:0000269|PubMed:10498708}.
CC   -!- MISCELLANEOUS: Bacterial microcompartments (BMC) 100-200 nm in cross
CC       section are formed during aerobic growth on minimal 1,2-PD-B12 or
CC       anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic
CC       growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate
CC       (PubMed:10498708). BMCs can constitute up to 10% of total cell protein
CC       (PubMed:12923081). {ECO:0000269|PubMed:10498708,
CC       ECO:0000269|PubMed:12923081}.
CC   -!- SIMILARITY: Belongs to the EutP/PduV family. {ECO:0000305}.
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DR   EMBL; AF026270; AAD39020.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20960.1; -; Genomic_DNA.
DR   RefSeq; NP_461001.1; NC_003197.2.
DR   RefSeq; WP_000826277.1; NC_003197.2.
DR   AlphaFoldDB; Q9XDM6; -.
DR   SMR; Q9XDM6; -.
DR   STRING; 99287.STM2056; -.
DR   PaxDb; Q9XDM6; -.
DR   EnsemblBacteria; AAL20960; AAL20960; STM2056.
DR   GeneID; 1253577; -.
DR   KEGG; stm:STM2056; -.
DR   PATRIC; fig|99287.12.peg.2178; -.
DR   HOGENOM; CLU_113298_2_0_6; -.
DR   OMA; TQAIVWS; -.
DR   PhylomeDB; Q9XDM6; -.
DR   BioCyc; SENT99287:STM2056-MON; -.
DR   UniPathway; UPA00621; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0031472; C:propanediol degradation polyhedral organelle; IPI:UniProtKB.
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;
KW   Reference proteome.
FT   CHAIN           1..150
FT                   /note="Propanediol utilization protein PduV"
FT                   /id="PRO_0000058281"
FT   BINDING         8..15
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000305|PubMed:25646976"
SQ   SEQUENCE   150 AA;  16348 MW;  7771229432F97E56 CRC64;
     MKRLMFIGPS QCGKTSLTQS LRGEALHYKK TQAIEWSPMA IDTPGEYLEN RCLYSALLTS
     ACEADVIALV LNADAQWSPF SPGFTAPMNR PTIGLVTKAD LAEPQRISLV AEWLTQAGAQ
     QIFITSALNN SGLDAVLDFL NSKEPLCLTK