THL_BACSU
ID THL_BACSU Reviewed; 393 AA.
AC P45855;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
GN Name=mmgA; Synonyms=yqiL; OrderedLocusNames=BSU24170;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=168 / MB24;
RX PubMed=8759838; DOI=10.1128/jb.178.16.4778-4786.1996;
RA Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT "A sigma E dependent operon subject to catabolite repression during
RT sporulation in Bacillus subtilis.";
RL J. Bacteriol. 178:4778-4786(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed in the mother cell at intermediate
CC stages of sporulation under the control of the sigma-E factor.
CC {ECO:0000269|PubMed:8759838}.
CC -!- INDUCTION: Subject to catabolite repression.
CC {ECO:0000269|PubMed:8759838}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; U29084; AAB09613.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12587.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14348.1; -; Genomic_DNA.
DR PIR; B69658; B69658.
DR RefSeq; NP_390297.1; NC_000964.3.
DR RefSeq; WP_003230291.1; NZ_JNCM01000036.1.
DR PDB; 5LP7; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-393.
DR PDBsum; 5LP7; -.
DR AlphaFoldDB; P45855; -.
DR SMR; P45855; -.
DR STRING; 224308.BSU24170; -.
DR PaxDb; P45855; -.
DR PRIDE; P45855; -.
DR EnsemblBacteria; CAB14348; CAB14348; BSU_24170.
DR GeneID; 938662; -.
DR KEGG; bsu:BSU24170; -.
DR PATRIC; fig|224308.179.peg.2631; -.
DR eggNOG; COG0183; Bacteria.
DR InParanoid; P45855; -.
DR OMA; TNVCCTT; -.
DR PhylomeDB; P45855; -.
DR BioCyc; BSUB:BSU24170-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Sporulation;
KW Transferase.
FT CHAIN 1..393
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206402"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT CONFLICT 68
FT /note="Q -> L (in Ref. 1; AAB09613)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 172..191
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 192..198
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 273..283
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5LP7"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:5LP7"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:5LP7"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:5LP7"
SQ SEQUENCE 393 AA; 41179 MW; E2D52259679E50F7 CRC64;
MRKTVIVSAA RTPFGKFGGV LKEVKAAELG GIVMKEALQQ AGVSGDDVEG NVMGMVVQAG
SGQIPSRQAA RLAGMPWSVP SETLNKVCAS GLRAVTLCDQ MIRAQDADIL VAGGMESMSN
IPYAVPAGRW GARMGDGELR DLMVYDGLTC AFDEVHMAVH GNTAAKEYAI SRREQDEWAL
RSHARAAKAA DEGKFQDEIV PVNWIGRKGK PNVVDKDEAI RRDTSLDQLA KLAPIYASDG
SITAGNAPGV NDGAGAFVLM SEEKAAELGK RPLATILGFS TTGMPAHELA AAPGFAINKL
LKKNGLTVQD IDLFEVNEAF ASVVLTCEKI VGFDLEKVNV NGGAIALGHP IGASGARILM
TLVYELKRRG GGLGVAAICS GAAQGDAVLV QVH
