ID A0A0D8FU40_9ACTN Unreviewed; 529 AA.
AC A0A0D8FU40;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KJE75757.1};
DE EC=6.3.2.10 {ECO:0000313|EMBL:KJE75757.1};
GN Name=murF {ECO:0000313|EMBL:KJE75757.1};
GN ORFNames=FEAC_25340 {ECO:0000313|EMBL:KJE75757.1};
OS Ferrimicrobium acidiphilum DSM 19497.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrimicrobium.
OX NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE75757.1, ECO:0000313|Proteomes:UP000032336};
RN [1] {ECO:0000313|EMBL:KJE75757.1, ECO:0000313|Proteomes:UP000032336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T23 {ECO:0000313|EMBL:KJE75757.1,
RC ECO:0000313|Proteomes:UP000032336};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Ferrimicrobium acidiphilum
RT strain T23.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJE75757.1}.
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DR EMBL; JXUW01000030; KJE75757.1; -; Genomic_DNA.
DR RefSeq; WP_035392389.1; NZ_JXUW01000030.1.
DR AlphaFoldDB; A0A0D8FU40; -.
DR STRING; 1121877.FEAC_25340; -.
DR GeneID; 78373554; -.
DR PATRIC; fig|1121877.4.peg.2826; -.
DR eggNOG; COG0770; Bacteria.
DR OrthoDB; 9800958at2; -.
DR Proteomes; UP000032336; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KJE75757.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032336};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..326
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 529 AA; 56111 MW; 6FA3200FD1647E4A CRC64;
MGHELAVVVA VLIGIVAQTP ALKWVRVGQR EHYLPGRIGP FFALWFRASF VNQALLVVGL
VLLVGSFVQS FGTEVHLVIA ALLVICLLLT PFGLGFRGRT SPLALTSRMR RLLVAVGLID
VIVTLVGLVV GLPLAFALLA GFFAPAVVEL ALIATRPLED HLLQRYVDDA TERLLRVRPR
VVGITGSFGK TTTKNYLATL LEGSVRAIAS PASFNNRGGL ARSINERLVP GTEVFVAEMG
TFGPGEIAAL CSWIPPEIAV LTALGPVHLE RFGSEASILR AKLEITEQAS VVIINIDYPR
LALAAKALAG SATDRRIVKV SAIQLDADVT VKPNEEGELV VYLHGQKLAK IDAGDIAPTN
LACAVAAALE CGVAPEALQS RLGLVKSPAN RLVTAVVPDS GVEVLDDTYN SNPAGARRAL
AALQRRGGEA ATKFVVTPGM VELGKRQYPE NYALGKAVGQ VANQLVVVGM TNRIALMEGA
AEAQATAEGT RLDAVVSVKD RDSAIAYIKR SAKSGDVVLY ENDLPDHYP
//
