ID   A2SGY9_METPP            Unreviewed;       560 AA.
AC   A2SGY9;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Putative poly-beta-hydroxybutyrate polymerase transmembrane protein {ECO:0000313|EMBL:ABM94828.1};
DE            EC=2.3.1.- {ECO:0000313|EMBL:ABM94828.1};
GN   OrderedLocusNames=Mpe_A1870 {ECO:0000313|EMBL:ABM94828.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM94828.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM94828.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CP000555; ABM94828.1; -; Genomic_DNA.
DR   RefSeq; WP_011829465.1; NC_008825.1.
DR   AlphaFoldDB; A2SGY9; -.
DR   STRING; 420662.Mpe_A1870; -.
DR   KEGG; mpt:Mpe_A1870; -.
DR   eggNOG; COG3243; Bacteria.
DR   HOGENOM; CLU_017387_3_0_4; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010963; PHA_synth_I.
DR   InterPro; IPR010941; PhaC_N.
DR   NCBIfam; TIGR01838; PHA_synth_I; 1.
DR   PANTHER; PTHR36837; POLY(3-HYDROXYALKANOATE) POLYMERASE SUBUNIT PHAC; 1.
DR   PANTHER; PTHR36837:SF2; POLY(3-HYDROXYALKANOATE) POLYMERASE SUBUNIT PHAC; 1.
DR   Pfam; PF07167; PhaC_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:ABM94828.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000313|EMBL:ABM94828.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABM94828.1};
KW   Transmembrane {ECO:0000313|EMBL:ABM94828.1}.
FT   DOMAIN          75..241
FT                   /note="Poly-beta-hydroxybutyrate polymerase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07167"
SQ   SEQUENCE   560 AA;  61888 MW;  2CC42D46C41FE2CE CRC64;
     MNKGATGWGG VAPGMDFAQS AQQLAQGWTE ALKGMTGVQL PADALPALQS SYLSEAAALW
     NQATQGADGA PPPADRRFAA KDWMSNPAAA FTAGMYMLNA RTLLQLADQV QADEKTRQRI
     RFAVQQWIDA SSPANYLALN PEAQRKAIET QGESITQGLQ HLWHDVRQGH LSQTDESLFE
     VGRNVATTEG SVVFENALFQ LIEYKPLTAK VHERPLLIVP PCINKFYIMD LQPENSLVRY
     AVSQGHRVFM LSWVNADESL GDKTWDDYIE HAVIRAIREV QAISKQEQIN TLGFCIGGTL
     LATALAVLAA RGEHPSASLT MLTSFLDFSD TGVLDLFVDE QMVSMREMAL GQGGLLKGKE
     LAATFSFLRP NDLVWNYVVG NYLKGETPPP FDLLYWNSDS TNLPGPMYCW YLRHTYLENN
     LIKPGKVTVC GEPLDLRKVN LPTFIYASRE DHIVPWQSAY ATVEVLPGKK QFVLGASGHI
     AGVINPPTKN KRSHWINSRL PKTADAWFEG ATEHPGSWWP AWTDWLKPLG GKLVPAPKAP
     GDRNHKIIEP APGRYVKAKA
//