ID   FABF_STAAC              Reviewed;         414 AA.
AC   Q5HHA1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SACOL0988;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW36456.1; -; Genomic_DNA.
DR   RefSeq; WP_000081240.1; NC_002951.2.
DR   PDB; 2GQD; X-ray; 2.30 A; A=1-414.
DR   PDBsum; 2GQD; -.
DR   AlphaFoldDB; Q5HHA1; -.
DR   SMR; Q5HHA1; -.
DR   EnsemblBacteria; AAW36456; AAW36456; SACOL0988.
DR   KEGG; sac:SACOL0988; -.
DR   HOGENOM; CLU_000022_69_2_9; -.
DR   OMA; YRYIKYK; -.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; Q5HHA1; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Transferase.
FT   CHAIN           1..414
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT                   /id="PRO_0000180320"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   414 AA;  43739 MW;  2DB06BB5DD48D175 CRC64;
     MSQNKRVVIT GMGALSPIGN DVKTTWENAL KGVNGIDKIT RIDTEPYSVH LAGELKNFNI
     EDHIDKKEAR RMDRFTQYAI VAAREAVKDA QLDINENTAD 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