ID T1ZG88_STRIT Unreviewed; 404 AA.
AC T1ZG88;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:AGU76472.1};
DE EC=2.3.2.- {ECO:0000313|EMBL:AGU76472.1};
GN Name=murM {ECO:0000313|EMBL:AGU76472.1};
GN ORFNames=SIR_1111 {ECO:0000313|EMBL:AGU76472.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU76472.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU76472.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU76472.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008694}.
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DR EMBL; CP003857; AGU76472.1; -; Genomic_DNA.
DR RefSeq; WP_021002938.1; NZ_UZBH01000001.1.
DR AlphaFoldDB; T1ZG88; -.
DR KEGG; sib:SIR_1111; -.
DR PATRIC; fig|862967.3.peg.1124; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_2_0_9; -.
DR OrthoDB; 2173585at2; -.
DR Proteomes; UP000016233; Chromosome.
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 Gene3D; 1.20.58.90; -; 1.
DR Gene3D; 3.40.630.30; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AGU76472.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000016233};
KW Transferase {ECO:0000313|EMBL:AGU76472.1}.
FT COILED 237..290
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 404 AA; 46645 MW; CAA4A83FBB178641 CRC64;
MYTYKIGISV QAHDDFVKQS SQINLLQSAS WAKVKDNWDN ERIGFYKNNQ LVASASILIK
PLPLSMTMLY IPRGPIMDYQ DQELLHFVLT SLKKFAKTKK ALFIKFDPSL FLVQNQSGEE
RQDNPKTLDL INNLQKAGAI WLGRTELLDE TIQPRFQANI YKDNFSEELL SKSTRQAIRT
ARNKGIQVQF GGSELLDDFS ALMKKTENRK SIHLRGQDYY QKLLDTYPEH SYITLASINL
NERLESLQVQ KSKAEKEASK FTEKTKPGKI ENNKQEQKRL QEEMDFLAEK MTQGAITVPL
SGTLVLEYGT TSENIYAGMD EEYRRYQPAI LTWYETAKHA FERGANWQNM GGVENDLDGG
LYHFKSKFNP TIEEYAGEFN LPTNPLYHLS NIAYTLRKKF RSKH
//
