ID D2EQA3_9STRE Unreviewed; 245 AA.
AC D2EQA3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Acyl-ACP thioesterase {ECO:0000313|EMBL:EFA24288.1};
GN ORFNames=HMPREF0850_00162 {ECO:0000313|EMBL:EFA24288.1};
OS Streptococcus sp. M143.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563037 {ECO:0000313|EMBL:EFA24288.1, ECO:0000313|Proteomes:UP000002766};
RN [1] {ECO:0000313|EMBL:EFA24288.1, ECO:0000313|Proteomes:UP000002766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M143 {ECO:0000313|EMBL:EFA24288.1,
RC ECO:0000313|Proteomes:UP000002766};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. strain M143.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family.
CC {ECO:0000256|ARBA:ARBA00006500}.
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; GG730097; EFA24288.1; -; Genomic_DNA.
DR RefSeq; WP_000524809.1; NZ_GG730097.1.
DR AlphaFoldDB; D2EQA3; -.
DR eggNOG; COG3884; Bacteria.
DR HOGENOM; CLU_045466_2_0_9; -.
DR OrthoDB; 9801517at2; -.
DR Proteomes; UP000002766; Unassembled WGS sequence.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00586; 4HBT; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR InterPro; IPR049427; Acyl-ACP_TE_C.
DR InterPro; IPR002864; Acyl-ACP_thioesterase_NHD.
DR InterPro; IPR045023; FATA/B.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR31727; OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31727:SF6; OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF01643; Acyl-ACP_TE; 1.
DR Pfam; PF20791; Acyl-ACP_TE_C; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 2..132
FT /note="Acyl-ACP thioesterase N-terminal hotdog"
FT /evidence="ECO:0000259|Pfam:PF01643"
FT DOMAIN 148..241
FT /note="Acyl-ACP thioesterase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20791"
SQ SEQUENCE 245 AA; 28395 MW; 6DF98AA3A8528314 CRC64;
MGLTYQMTMK IPFDMADMNG HIKLPDVILL SLQVSGMQSI ELGVSDKDVL ERYNLVWIIT
DYAIDVVRLP RFAEEITIET EALTYNRLFC YRRFTIYDEA GQEIIRMVAT FVLMDRDSRK
VHAVEPEIVA PYQSEFDKKL IRGPKYANLE DPISKDYHVR FYDLDMNGHV NNSKYLDWIF
EVMGADFLTK YIPKKINLKY VKEVRPGGMI ASAYELNGLE SKHEIISDGE INAQAMITWQ
EIKGN
//
