ID   FABF_STAAM              Reviewed;         414 AA.
AC   Q99VA6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2;
DE            EC=2.3.1.179 {ECO:0000250|UniProtKB:P0AAI5};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II;
DE   AltName: Full=Beta-ketoacyl-ACP synthase II;
DE            Short=KAS II;
GN   Name=fabF; OrderedLocusNames=SAV0984;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC       Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC       two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC       catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC       to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC       the thermal regulation of fatty acid composition.
CC       {ECO:0000250|UniProtKB:P0AAI5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC         octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC         Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC         ChEBI:CHEBI:138538; EC=2.3.1.179;
CC         Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P0AAI5}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB57146.1; -; Genomic_DNA.
DR   RefSeq; WP_000081231.1; NC_002758.2.
DR   AlphaFoldDB; Q99VA6; -.
DR   SMR; Q99VA6; -.
DR   World-2DPAGE; 0002:Q99VA6; -.
DR   PaxDb; Q99VA6; -.
DR   EnsemblBacteria; BAB57146; BAB57146; SAV0984.
DR   KEGG; sav:SAV0984; -.
DR   HOGENOM; CLU_000022_69_2_9; -.
DR   OMA; YRYIKYK; -.
DR   PhylomeDB; Q99VA6; -.
DR   BioCyc; SAUR158878:SAV_RS05330-MON; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712; PTHR11712; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000447; KAS_II; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR03150; fabF; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Transferase.
FT   CHAIN           1..414
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT                   /id="PRO_0000180321"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   414 AA;  43725 MW;  46C0005B584824C5 CRC64;
     MSQNKRVVIT GMGALSPIGN DVKTTWENAL KGVNGIDKIT RIDTEPYSVH LAGELKNFNI
     EDHIDKKEAR RMDRFTQYAI VAAREAVKDA QLDINDNTAD RIGVWIGSGI GGMETFEIAH
     KQLMDKGPRR VSPFFVPMLI PDMATGQVSI DLGAKGPNGA TVTACATGTN SIGEAFKIVQ
     RGDADAMITG GTEAPITHMA IAGFSASRAL STNDDIETAC RPFQEGRDGF VMGEGAGILV
     IESLESAQAR GANIYAEIVG YGTTGDAYHI TAPAPEGEGG SRAMQAAMDD AGIEPKDVQY
     LNAHGTSTPV GDLNEVKAIK NTFGEAAKHL KVSSTKSMTG HLLGATGGIE AIFSALSIKD
     SKVAPTIHAV TPDPECDLDI VPNEAQDLDI TYAMSNSLGF GGHNAVLVFK KFEA