ID A0A0W0WLI5_9GAMM Unreviewed; 612 AA.
AC A0A0W0WLI5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Poly-beta-hydroxybutyrate polymerase {ECO:0000313|EMBL:KTD33178.1};
GN ORFNames=Lnau_2826 {ECO:0000313|EMBL:KTD33178.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD33178.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD33178.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD33178.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KTD33178.1}.
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DR EMBL; LNYO01000024; KTD33178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0WLI5; -.
DR STRING; 45070.Lnau_2826; -.
DR PATRIC; fig|45070.6.peg.2980; -.
DR OrthoDB; 7208816at2; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
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; IPR000073; AB_hydrolase_1.
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; PF00561; Abhydrolase_1; 1.
DR Pfam; PF07167; PhaC_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 92..263
FT /note="Poly-beta-hydroxybutyrate polymerase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07167"
FT DOMAIN 264..508
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 580..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 70528 MW; AD57C8D899B4BA1C CRC64;
MTQDTELSDI MRSVAEKSMR ILQEVSQQPA QLSKLVKEYM DLTKEFQLLV AVILKNPEQV
WQMQIAYWQD ALTLAHEQLN YWMEGKSMPI TDRRFSSEEW VNNPFFNFMS QHYLLASEHM
NSLLEHIEYG DKQLARRVQF FTRQYLDALS PANFLHTNPQ LMAETVQSHG KNLLRGLQNL
LTDMESGSSR LIIKMTDTDA FKVGKNLATT PGKVVFRNEM MELIQYTPQT EKVRSIPLLM
IPPWINKYYI LDLSENNSLV GWLVKQGITV FIISWINPDA SYAEKGLFDY LQDGPMAAIK
IMQEQLKVKQ VNTLGFCIGG TLLACMLAYQ KAHHEKPVRS ATFLASMIDF SDPGDISVFI
DEQQIVRIEE EMHSKGFLDG RFMASTFNSL RANDLVWSFF IKNYLQGQNP VPFDILYWNA
DVTNMPAKMH SQYLRWMYLH NDLVKPGKIR LNQVPLDVSQ IDIPTFFVST KKDHIAPWQT
TYLGFQHMSG KKRFLLGGSG HIAGIVNPPG NDKYGYYHNT STTQTMDEWL EKAKERPGSW
WPEWLKWLEK ESGRIVDAPS FEQLPYKGLM DAPGKYVHKT YKTPKQDEPN EETATVDKDI
YTETNNGVNT AA
//
