FEMA_STAAU
ID FEMA_STAAU Reviewed; 420 AA.
AC P0A0A5; P14304;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Aminoacyltransferase FemA;
DE EC=2.3.2.17;
DE AltName: Full=Factor essential for expression of methicillin resistance A;
DE AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase;
GN Name=femA;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2559314; DOI=10.1007/bf00261186;
RA Berger-Baechi B., Barberis-Maino L., Straessle A., Kayser F.H.;
RT "FemA, a host-mediated factor essential for methicillin resistance in
RT Staphylococcus aureus: molecular cloning and characterization.";
RL Mol. Gen. Genet. 219:263-269(1989).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=SG511;
RX PubMed=7590176; DOI=10.1111/j.1574-6968.1995.tb07837.x;
RA Johnson S., Krueger D., Labischinski H.;
RT "FemA of Staphylococcus aureus: isolation and immunodetection.";
RL FEMS Microbiol. Lett. 132:221-228(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=12176388; DOI=10.1016/s0969-2126(02)00807-9;
RA Benson T.E., Prince D.B., Mutchler V.T., Curry K.A., Ho A.M., Sarver R.W.,
RA Hagadorn J.C., Choi G.H., Garlick R.L.;
RT "X-ray crystal structure of Staphylococcus aureus FemA.";
RL Structure 10:1107-1115(2002).
CC -!- FUNCTION: Catalyzes the formation of the pentaglycine interpeptide
CC bridge, which is characteristic of the S.aureus peptidoglycan. Adds
CC glycines 2 and 3 of the pentaglycine bridge, using glycyl-tRNA(Gly) as
CC donor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-
CC (N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate +
CC 2 glycyl-tRNA(Gly) = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-
CC (N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-
CC GlcNAc + 2 tRNA(Gly); Xref=Rhea:RHEA:30439, Rhea:RHEA-COMP:9664,
CC Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62234,
CC ChEBI:CHEBI:62235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.17;
CC -!- SUBUNIT: Homodimer. Interacts with FemB (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7590176}.
CC -!- MISCELLANEOUS: Since cross-linking between the peptide strands is
CC critical for maintaining stability of the cell wall, FemA is a
CC potential target for the development of new antibacterial agents.
CC -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35679.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17688; CAA35679.1; ALT_INIT; Genomic_DNA.
DR PIR; S06783; S06783.
DR RefSeq; WP_000673309.1; NZ_WOFG01000001.1.
DR PDB; 1LRZ; X-ray; 2.10 A; A=1-420.
DR PDBsum; 1LRZ; -.
DR AlphaFoldDB; P0A0A5; -.
DR SMR; P0A0A5; -.
DR OMA; YNFLGIM; -.
DR BioCyc; MetaCyc:MON-15453; -.
DR BRENDA; 2.3.2.17; 3352.
DR EvolutionaryTrace; P0A0A5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR InterPro; IPR010978; tRNA-bd_arm.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55729; SSF55729; 2.
DR PROSITE; PS51191; FEMABX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW Transferase.
FT CHAIN 1..420
FT /note="Aminoacyltransferase FemA"
FT /id="PRO_0000204735"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 52..63
FT /evidence="ECO:0007829|PDB:1LRZ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:1LRZ"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 245..272
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 277..307
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 309..320
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:1LRZ"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:1LRZ"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:1LRZ"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:1LRZ"
SQ SEQUENCE 420 AA; 49124 MW; E6790BD7C8B50297 CRC64;
MKFTNLTAKE FGAFTDSMPY SHFTQTVGHY ELKLAEGYET HLVGIKNNNN EVIAACLLTA
VPVMKVFKYF YSNRGPVIDY ENQELVHFFF NELSKYVKKH RCLYLHIDPY LPYQYLNHDG
EITGNAGNDW FFDKMSNLGF EHTGFHKGFD PVLQIRYHSV LDLKDKTADD IIKNMDGLRK
RNTKKVKKNG VKVRFLSEEE LPIFRSFMED TSESKAFADR DDKFYYNRLK YYKDRVLVPL
AYINFDEYIK ELNEERDILN KDLNKALKDI EKRPENKKAH NKRDNLQQQL DANEQKIEEG
KRLQEEHGNE LPISAGFFFI NPFEVVYYAG GTSNAFRHFA GSYAVQWEMI NYALNHGIDR
YNFYGVSGKF TEDAEDAGVV KFKKGYNAEI IEYVGDFIKP INKPVYAAYT ALKKVKDRIF
