ID   YDCS_ECOLI              Reviewed;         381 AA.
AC   P76108; Q2MBB6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Bifunctional polyhydroxybutyrate synthase / ABC transporter periplasmic binding protein {ECO:0000305};
DE   AltName: Full=Poly-3-hydroxybutyrate synthase {ECO:0000303|PubMed:18640095};
DE            Short=PHB synthase {ECO:0000303|PubMed:18640095};
DE            EC=2.3.1.- {ECO:0000269|PubMed:18640095};
DE   AltName: Full=cPHB synthase {ECO:0000303|PubMed:18640095};
DE   Flags: Precursor;
GN   Name=ydcS; OrderedLocusNames=b1440, JW1435;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION AS A PHB SYNTHASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18640095; DOI=10.1016/j.bbrc.2008.07.043;
RA   Dai D., Reusch R.N.;
RT   "Poly-3-hydroxybutyrate synthase from the periplasm of Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 374:485-489(2008).
RN   [4]
RP   INDUCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=23531166; DOI=10.1111/mmi.12207;
RA   Schneider B.L., Hernandez V.J., Reitzer L.;
RT   "Putrescine catabolism is a metabolic response to several stresses in
RT   Escherichia coli.";
RL   Mol. Microbiol. 88:537-550(2013).
RN   [5]
RP   FUNCTION IN TRANSFORMATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26826386; DOI=10.1016/j.bbrc.2016.01.137;
RA   Sun D.;
RT   "Two different routes for double-stranded DNA transfer in natural and
RT   artificial transformation of Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 471:213-218(2016).
CC   -!- FUNCTION: Catalyzes the formation of short polymers of R-3-
CC       hydroxybutyrate (cPHB) (PubMed:18640095). Involved in natural
CC       transformation (PubMed:26826386). Probably part of the ABC transporter
CC       complex YdcSTUV. During natural transformation, may bind dsDNA and
CC       convey it to the inner membrane channel formed by YdcV (Probable).
CC       {ECO:0000269|PubMed:18640095, ECO:0000269|PubMed:26826386,
CC       ECO:0000305|PubMed:26826386}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-3-hydroxybutanoyl-CoA + [(3R)-hydroxybutanoate](n) =
CC         [(3R)-hydroxybutanoate](n+1) + CoA; Xref=Rhea:RHEA:15405, Rhea:RHEA-
CC         COMP:14464, Rhea:RHEA-COMP:14465, ChEBI:CHEBI:8298,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57315;
CC         Evidence={ECO:0000269|PubMed:18640095};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.14 mM for 3-hydroxybutyryl-CoA {ECO:0000269|PubMed:18640095};
CC         Vmax=18.7 nmol/min/mg enzyme {ECO:0000269|PubMed:18640095};
CC       pH dependence:
CC         Optimum pH is 6.8-7.8. {ECO:0000269|PubMed:18640095};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:18640095};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:18640095}.
CC   -!- INDUCTION: Induced under nitrogen-limited growth.
CC       {ECO:0000269|PubMed:23531166}.
CC   -!- DISRUPTION PHENOTYPE: The deletion mutant contains 30% less cPHB in the
CC       outer membrane than the wild-type strain (PubMed:18640095). Natural
CC       transformation rate of the mutant is reduced by 2.7-6.7 folds. Mutant
CC       is also defective in chemical transformation (PubMed:26826386).
CC       {ECO:0000269|PubMed:18640095, ECO:0000269|PubMed:26826386}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein PotD/PotF
CC       family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74522.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76440.1; -; Genomic_DNA.
DR   PIR; C64896; C64896.
DR   RefSeq; NP_415957.1; NC_000913.3.
DR   RefSeq; WP_000047424.1; NZ_SSZK01000021.1.
DR   AlphaFoldDB; P76108; -.
DR   SMR; P76108; -.
DR   BioGRID; 4262896; 55.
DR   ComplexPortal; CPX-4446; YdcSTUV ABC transporter complex.
DR   IntAct; P76108; 19.
DR   STRING; 511145.b1440; -.
DR   TCDB; 3.A.1.11.9; the atp-binding cassette (abc) superfamily.
DR   jPOST; P76108; -.
DR   PaxDb; 511145-b1440; -.
DR   EnsemblBacteria; AAC74522; AAC74522; b1440.
DR   GeneID; 75171521; -.
DR   GeneID; 946005; -.
DR   KEGG; ecj:JW1435; -.
DR   KEGG; eco:b1440; -.
DR   PATRIC; fig|1411691.4.peg.828; -.
DR   EchoBASE; EB3525; -.
DR   eggNOG; COG0687; Bacteria.
DR   HOGENOM; CLU_026974_1_5_6; -.
DR   InParanoid; P76108; -.
DR   OMA; YDWVTGF; -.
DR   OrthoDB; 9813777at2; -.
DR   PhylomeDB; P76108; -.
DR   BioCyc; EcoCyc:YDCS-MONOMER; -.
DR   BioCyc; MetaCyc:YDCS-MONOMER; -.
DR   PRO; PR:P76108; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal.
DR   GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019808; F:polyamine binding; IEA:InterPro.
DR   GO; GO:0009290; P:DNA import into cell involved in transformation; IMP:EcoCyc.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IDA:EcoCyc.
DR   GO; GO:0015846; P:polyamine transport; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; NAS:ComplexPortal.
DR   CDD; cd13588; PBP2_polyamine_1; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR006059; SBP.
DR   InterPro; IPR001188; Sperm_putr-bd.
DR   NCBIfam; NF041888; ABC_SBP_YdcS; 1.
DR   PANTHER; PTHR30222:SF17; BIFUNCTIONAL POLYHYDROXYBUTYRATE SYNTHASE _ ABC TRANSPORTER PERIPLASMIC BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR30222; SPERMIDINE/PUTRESCINE-BINDING PERIPLASMIC PROTEIN; 1.
DR   Pfam; PF13416; SBP_bac_8; 1.
DR   PRINTS; PR00909; SPERMDNBNDNG.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Periplasm; PHB biosynthesis; Reference proteome; Signal;
KW   Transferase; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..381
FT                   /note="Bifunctional polyhydroxybutyrate synthase / ABC
FT                   transporter periplasmic binding protein"
FT                   /id="PRO_0000031843"
SQ   SEQUENCE   381 AA;  42295 MW;  FC5072B0B52CFB05 CRC64;
     MSKTFARSSL CALSMTIMTA HAAEPPTNLD KPEGRLDIIA WPGYIERGQT DKQYDWVTQF
     EKETGCAVNV KTAATSDEMV SLMTKGGYDL VTASGDASLR LIMGKRVQPI NTALIPNWKT
     LDPRVVKGDW FNVGGKVYGT PYQWGPNLLM YNTKTFPTPP DSWQVVFVEQ NLPDGKSNKG
     RVQAYDGPIY IADAALFVKA TQPQLGISDP YQLTEEQYQA VLKVLRAQHS LIHRYWHDTT
     VQMSDFKNEG VVASSAWPYQ ANALKAEGQP VATVFPKEGV TGWADTTMLH SEAKHPVCAY
     KWMNWSLTPK VQGDVAAWFG SLPVVPEGCK ASPLLGEKGC ETNGFNYFDK IAFWKTPIAE
     GGKFVPYSRW TQDYIAIMGG R
//