ID A0A0W0VDK7_9GAMM Unreviewed; 620 AA.
AC A0A0W0VDK7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Poly-beta-hydroxybutyrate polymerase {ECO:0000313|EMBL:KTD18199.1};
GN ORFNames=Ljor_2505 {ECO:0000313|EMBL:KTD18199.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD18199.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD18199.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD18199.1,
RC ECO:0000313|Proteomes:UP000055035};
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:KTD18199.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYJ01000011; KTD18199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VDK7; -.
DR STRING; 456.Ljor_2505; -.
DR PATRIC; fig|456.5.peg.2693; -.
DR OrthoDB; 7208816at2; -.
DR Proteomes; UP000055035; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000055035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 91..263
FT /note="Poly-beta-hydroxybutyrate polymerase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07167"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 70624 MW; 528A434236A60E63 CRC64;
MTQDTELSDL MQSVALKSLQ LIDSFKQQPA QTPALLKQFF DLTTSFQDLL TIILKNPEKL
WQMQLAYLQD AMSLAQEQFK HWLEGKPMPI EDKRFNGDEW VNNPFFNLLS QHYLLASEHL
NCLLENLDYG DKQLAKRVQF FTRQYLDALS PANFLHTNPQ LMAETIQSHG KNLLRGLKNL
LTDMESGSSR LIIKMTDTDA FKIGSNIATT PGKIIFRNDM MELIQYSPQT ESVRSIPLLI
VPPWINKYYI LDLSPHNSFV KWLVQQGITV FMISWVNPDA SYARKGIFDY LNEGPLTAIK
TIQRQLGVKQ VNILGFCIGG TLVACLLAYL KALGEKPIRT ATFLASMIDF SDPGDISVFI
DEQQIVRIEE EMHAKGFLDG RFMASTFNSL RANDLVWSFF VKNYLQGKNP VPFDILYWNA
DATNMPAKMH SQYLRWMYLH NHLVKPGKIH LNHVPLDVTQ IDIPTFFVST QKDHIAPWKT
TYMGFQLMKG KKRFLLGGSG HIAGIVNPPT SGKYGFYRNS SSNQSAEEWL ANAKHQPGSW
WPEWLNWLEK QAGEVIPAPD FKQLPLKGIM DAPGEYVRKV YKDVMQNNEQ PAEVLFLKDL
NDSESKPVPA SENTTAAGSK
//