ID   FABZ_STRR6              Reviewed;         140 AA.
AC   P59202; Q9FBC0;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ;
DE            EC=4.2.1.59;
DE   AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase;
DE            Short=(3R)-hydroxymyristoyl-ACP dehydrase;
DE   AltName: Full=Beta-hydroxyacyl-ACP dehydratase;
GN   Name=fabZ; OrderedLocusNames=spr0384;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10910344; DOI=10.1038/35018162;
RA   Heath R.J., Rock C.O.;
RT   "A triclosan-resistant bacterial enzyme.";
RL   Nature 406:145-146(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
CC   -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes
CC       the dehydration of short chain beta-hydroxyacyl-ACPs and long chain
CC       saturated and unsaturated beta-hydroxyacyl-ACPs (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF197933; AAF98278.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAK99188.1; -; Genomic_DNA.
DR   PIR; H97919; H97919.
DR   RefSeq; NP_357978.1; NC_003098.1.
DR   RefSeq; WP_000565514.1; NC_003098.1.
DR   AlphaFoldDB; P59202; -.
DR   SMR; P59202; -.
DR   STRING; 171101.spr0384; -.
DR   EnsemblBacteria; AAK99188; AAK99188; spr0384.
DR   GeneID; 60233764; -.
DR   KEGG; spr:spr0384; -.
DR   PATRIC; fig|171101.6.peg.425; -.
DR   eggNOG; COG0764; Bacteria.
DR   HOGENOM; CLU_078912_3_0_9; -.
DR   OMA; FPGRPLM; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00406; FabZ; 1.
DR   InterPro; IPR013114; FabA_FabZ.
DR   InterPro; IPR010084; FabZ.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   PANTHER; PTHR30272; PTHR30272; 1.
DR   Pfam; PF07977; FabA; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   TIGRFAMs; TIGR01750; fabZ; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Lyase; Reference proteome.
FT   CHAIN           1..140
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_0000091742"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000250"
FT   CONFLICT        58
FT                   /note="L -> V (in Ref. 1; AAF98278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="I -> T (in Ref. 1; AAF98278)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15298 MW;  6646401713F382B8 CRC64;
     MIDIQGIKEA LPHRYPMLLV DRVLEVSEDT IVAIKNVTIN EPFFNGHFPQ YPVMPGVLIM
     EALAQTAGVL ELSKPENKGK LVFYAGMDKV KFKKQVVPGD QLVMTATFVK RRGTIAVVEA
     KAEVDGKLAA SGILTFAIGN