ID   MENE_STAAE              Reviewed;         492 AA.
AC   A6QHX6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=2-succinylbenzoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00731};
DE            EC=6.2.1.26 {ECO:0000255|HAMAP-Rule:MF_00731};
DE   AltName: Full=o-succinylbenzoyl-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
DE            Short=OSB-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
GN   Name=menE {ECO:0000255|HAMAP-Rule:MF_00731}; OrderedLocusNames=NWMN_1686;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
CC   -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC       (OSB-CoA). {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:17009, ChEBI:CHEBI:18325,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57364, ChEBI:CHEBI:456215; EC=6.2.1.26;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00731};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 5/7.
CC       {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00731}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       MenE subfamily. {ECO:0000255|HAMAP-Rule:MF_00731}.
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DR   EMBL; AP009351; BAF67958.1; -; Genomic_DNA.
DR   RefSeq; WP_000348360.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QHX6; -.
DR   SMR; A6QHX6; -.
DR   EnsemblBacteria; BAF67958; BAF67958; NWMN_1686.
DR   KEGG; sae:NWMN_1686; -.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00166.
DR   Proteomes; UP000006386; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_00731; MenE; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR010192; MenE.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR01923; menE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Menaquinone biosynthesis; Nucleotide-binding.
FT   CHAIN           1..492
FT                   /note="2-succinylbenzoate--CoA ligase"
FT                   /id="PRO_1000072786"
SQ   SEQUENCE   492 AA;  55415 MW;  36D409105A4F7930 CRC64;
     MDFWLYKQAQ QNGHHIAITD GQESYTYQNL YCEASLLAKR LKAYQQSRVG LYIDNSIQSI
     ILIHACWLAN IEIAMINTRL TPNEMTNQMK SIDVQLIFCT LPLELRGFQI VSLDDIEFAG
     RDITTNSLLD NTMGIQYETS NETVVPKESP SNILNTSFNL DDIASIMFTS GTTGPQKAVP
     QTFRNHYASA IGCKESLGFD RDTNWLSVLP IYHISGLSVL LRAVIEGFTV RIVDKFNAEQ
     ILTMIKNERI THISLVPQTL NWLMQQGLHE PYNLQKILLG GAKLSATMIE TALQYNLPIY
     NSFGMTETCS QFLTATPEML HARPDTVGMP SANVDVKIKN PNKEGHGELM IKGANVMNVY
     LYPTDLTGTF ENGYFNTGDI AEIDHEGYVM IYDRRKDLII SGGENIYPYQ IETVAKQFPG
     ISDAVCVGHP DDTWGQVPKL YFVSESDISK AQLIAYLSQH LAKYKVPKHF EKVDTLPYTS
     TGKLQRNKLY RG