ID E8PLZ7_THESS Unreviewed; 340 AA.
AC E8PLZ7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=MurM {ECO:0000313|EMBL:ADW22416.1};
GN Name=murM {ECO:0000313|EMBL:ADW22416.1};
GN OrderedLocusNames=TSC_c18020 {ECO:0000313|EMBL:ADW22416.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW22416.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW22416.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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DR EMBL; CP001962; ADW22416.1; -; Genomic_DNA.
DR RefSeq; WP_015717681.1; NC_014974.1.
DR AlphaFoldDB; E8PLZ7; -.
DR STRING; 743525.TSC_c18020; -.
DR KEGG; tsc:TSC_c18020; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_0_1_0; -.
DR Proteomes; UP000008087; 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; 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; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
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 340 AA; 38032 MW; 4D3A9F1D24921668 CRC64;
MAELLEITDP EAWNRMVSSL PITSALQSWG WGEVKRLSGW VPRRLAVYGK EGLLGAAQVL
LRPLPGGLRL AYAPRGPALS RLEDLPLVAR ALAQGVRGTH LVLEPEAGWP AEEPPPTFPG
LLLEESIQPA YSLWLDLTQG EEALLKGMKE MHRRNARLAL KRTELGVEGE EAFPEFFHLF
EETNRRAKLL QHAKEYYQAV LREMNQPYGE AFLAVARKDG EALAAGLFVA FAGKVDYLYG
GSSRAHPEAK APMGMHLAAI RHGIGRGYRI YDLWGVPRTP EGSHAEGIWR FKEGFGGRRV
HFPAYTLPLS PLYRPLKLLL RLRKTWVNLR VRGNPRDVLG
//
