ID   FEMX_STAS1              Reviewed;         415 AA.
AC   Q49ZI0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Lipid II:glycine glycyltransferase;
DE            EC=2.3.2.16;
DE   AltName: Full=Factor essential for expression of methicillin resistance X;
GN   Name=femX; Synonyms=fmhB; OrderedLocusNames=SSP0651;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- FUNCTION: Catalyzes the incorporation of amino acid(s) into the
CC       interchain peptide bridge of peptidoglycan, using aminoacyl-tRNA as
CC       amino acid donor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-
CC         Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + glycyl-
CC         tRNA(Gly) = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-
CC         Lys-(N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
CC         diphosphate + H(+) + tRNA(Gly); Xref=Rhea:RHEA:30435, Rhea:RHEA-
CC         COMP:9664, Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62233,
CC         ChEBI:CHEBI:62234, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.16;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FemABX family. {ECO:0000305}.
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DR   EMBL; AP008934; BAE17796.1; -; Genomic_DNA.
DR   RefSeq; WP_011302589.1; NZ_MTGA01000036.1.
DR   AlphaFoldDB; Q49ZI0; -.
DR   SMR; Q49ZI0; -.
DR   STRING; 342451.SSP0651; -.
DR   EnsemblBacteria; BAE17796; BAE17796; SSP0651.
DR   KEGG; ssp:SSP0651; -.
DR   PATRIC; fig|342451.11.peg.653; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_0_1_9; -.
DR   OMA; FGLIQFK; -.
DR   OrthoDB; 891566at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016755; F:aminoacyltransferase activity; 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   Pfam; PF02388; FemAB; 1.
DR   SUPFAM; SSF55729; SSF55729; 2.
DR   PROSITE; PS51191; FEMABX; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Peptidoglycan synthesis; Reference proteome; Transferase.
FT   CHAIN           1..415
FT                   /note="Lipid II:glycine glycyltransferase"
FT                   /id="PRO_0000236179"
SQ   SEQUENCE   415 AA;  47525 MW;  C9AEE473126D95D8 CRC64;
     MEKMNITDQA HDAFVKAHPQ GDLLQLTQWA ETKTLTGWYS RRIAVGEDDE IVGVAQLLFK
     KVPKLPYTLC YISRGFVTDY SNKLALETLL EAAMQIAKEE KAYAIKIDPD VEVDKGADAL
     SNLRALGFKH KGFKEGLSKD YIQPRMTMIT PIEKTDVALI QSFERRNRSK VRLALKRGTT
     VERSNREGLK TFANLMQITG ERDGFLTRDI SYFENIYDAL HPDGDAELFL VKLEPKPVLE
     DLRQELHELE DEKAKLADKK QDKKTLNKIN DADNKIAKTQ ELIDEMVTLE STHPEGIYLS
     GALLMFAGKK SYYLYGASSN EYRNFLPNHH MQFAMMQYAR EHGATSYDFG GTDNNPDKDS
     DHYGLWTFKK VWGTYLSEKI GEFDYVLNAP LYQIIENIKP KLTKAKIKLS RKLKK