ID   FABF_STAAU              Reviewed;         403 AA.
AC   Q5TKS0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
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;
DE   Flags: Fragment;
GN   Name=fabF;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Smith;
RA   Morita Y., Ikeno S., Tsuchiya K.S.;
RT   "Cloning and expression of Staphylococcus aureus Smith fab genes.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; AB195291; BAD72839.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5TKS0; -.
DR   SMR; Q5TKS0; -.
DR   BindingDB; Q5TKS0; -.
DR   ChEMBL; CHEMBL5341; -.
DR   UniPathway; UPA00094; -.
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; -; 2.
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..>403
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT                   /id="PRO_0000180319"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   NON_TER         1
FT   NON_TER         403
SQ   SEQUENCE   403 AA;  42434 MW;  3600210DD4EC612E CRC64;
     VITGMGALSP IGNDVKTTWE NALKGVNGID KITRIDTEPY SVHLAGELKN FNIEDHIDKK
     EARRMDRFTQ YAIVAAREAV KDAQLDINEN TADRIGVWIG SGIGGMETFE IAHKQLMDKG
     PRRVSPFFVP MLIPDMATGQ VSIDLGAKGP NGATVTACAT GTNSIGEAFK IVQRGDADAM
     ITGGTEAPIT HMAIAGFSAS RALSTNDDIE TACRPFQEGR DGFVMGEGAG ILVIESLESA
     QARGANIYAE IVGYGTTGDA YHITAPAPEG EGGSRAMQAA MDDAGIEPKD VQYLNAHGTS
     TPVGDLNEVK AIKNTFGEAA KHLKVSSTKS MTGHLLGATG GIEAIFSALS IKDSKIAPTI
     HAVTPDPECD LDIVPNEAQD LDITYAMSNS LGFGGHNAVL VFK