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Database: UniProt
Entry: K8MVA0_9STRE
LinkDB: K8MVA0_9STRE
Original site: K8MVA0_9STRE 
ID   K8MVA0_9STRE            Unreviewed;       411 AA.
AC   K8MVA0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Aminoacyltransferase FemA {ECO:0000256|ARBA:ARBA00016236};
DE            EC=2.3.2.17 {ECO:0000256|ARBA:ARBA00012466};
DE   AltName: Full=Factor essential for expression of methicillin resistance A {ECO:0000256|ARBA:ARBA00032233};
DE   AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase {ECO:0000256|ARBA:ARBA00030706};
GN   ORFNames=HMPREF9186_00640 {ECO:0000313|EMBL:EKS20064.1};
OS   Streptococcus sp. F0442.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=999425 {ECO:0000313|EMBL:EKS20064.1, ECO:0000313|Proteomes:UP000001140};
RN   [1] {ECO:0000313|EMBL:EKS20064.1, ECO:0000313|Proteomes:UP000001140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0442 {ECO:0000313|EMBL:EKS20064.1,
RC   ECO:0000313|Proteomes:UP000001140};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Baranova O.V.,
RA   Mathney J., Dewhirst F.E., Izard J., Tanner A.C., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Streptococcus sp. F0442.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00023962};
CC   -!- SIMILARITY: Belongs to the FemABX family.
CC       {ECO:0000256|ARBA:ARBA00009943}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008694}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKS20064.1}.
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DR   EMBL; AGZZ01000004; EKS20064.1; -; Genomic_DNA.
DR   RefSeq; WP_009731381.1; NZ_KB373314.1.
DR   AlphaFoldDB; K8MVA0; -.
DR   STRING; 999425.HMPREF9186_00640; -.
DR   PATRIC; fig|999425.3.peg.636; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_048411_1_0_9; -.
DR   OrthoDB; 2303924at2; -.
DR   Proteomes; UP000001140; Unassembled WGS sequence.
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   Gene3D; 1.20.58.90; -; 1.
DR   Gene3D; 3.40.630.30; -; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR003447; FEMABX.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR36174:SF2; AMINOACYLTRANSFERASE FEMA; 1.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF02388; FemAB; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS51191; FEMABX; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
SQ   SEQUENCE   411 AA;  47653 MW;  B968BE88D9275AE8 CRC64;
     MTFAILTQKE FASHANSASY RSFMQTPEMA SLLEKRGFKI QYVGWKTGTQ ITISALLYSI
     PMTGGFHIEV NCGPVITDRS HLQDFYQSLQ DYAKNQGALE LIIKPYDTYQ TFNSDGNPIS
     EPNQDYINEL THIGYSFDGL QTGYPGGEPD WHYVKDMEGI TEKDLLKSFS KKGKPLVKKA
     KSFGMKLKRL NRDELQLFKD ITSSTSDRRN YLDKTLDYYQ TFYDSFGDKA DFMVATLNFH
     DYYTNLEKDQ GKLAQKIEKL QKDLEVNPHS EKKQNQLREF SSQFETFEVR KKEAKEYIEK
     YGDQDVILAG SLFVYMPQES TYLFSGSYTE FNKFYAPAVL QEYMMLETIK RGIPRYNFLG
     IQGIFDGSDG VLRFKQNFNG YIVRKMGTFR YYPNPLKFKA LSLIKRILGR S
//
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