ID A0A1H5SNX5_9CLOT Unreviewed; 531 AA.
AC A0A1H5SNX5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:SEF52296.1};
GN ORFNames=SAMN05660865_00435 {ECO:0000313|EMBL:SEF52296.1};
OS Caloramator fervidus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=29344 {ECO:0000313|EMBL:SEF52296.1, ECO:0000313|Proteomes:UP000242850};
RN [1] {ECO:0000313|Proteomes:UP000242850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5463 {ECO:0000313|Proteomes:UP000242850};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNUK01000003; SEF52296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5SNX5; -.
DR Proteomes; UP000242850; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR004101; Mur_ligase_C.
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; PF02875; Mur_ligase_C; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:SEF52296.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242850};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..376
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 396..475
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 531 AA; 60751 MW; 2DA46A9A1A872131 CRC64;
MIFVSILFFA FVSIYYNRFY LHMAQLVGYK PNEFLNWMNK YDKNNLRRNT ILLFLLFICY
LFPQRTGNIV LLTAWILISS INIYTHYKTR KKAKKPLKFT YRAIRLFTCA LFVNFILAFL
TYFVFKSFQA FLNGLILIQV FISYLMLLSL KLMLPIEKLI QQKFINEARE IIRRRKDLLV
IGVTGSYGKT STKYFIKTIL SEKYNTIMTP ESYNTPMGVT KVVREQLKNE HEIFVCEMGA
RYVGDIKELC EIVYPKIGVL TAVGLQHLET MGSKENIAKT KYELIESLPD DGIAFFNGDN
DICFELSKKR NIETYVYGTS KKEGINIYAT DIKNTKEGLK FTVCGNVDGR CVNFECKTKL
LGRHNVNNIL AGVAVALKLG LSEEEIKRGI EKIEPVPHRL QILDTNNGIT VIDDAFNSNP
EGASQALEAL SEMEGGKKII VTPGMIELGD AECEENKKFG KKIAEVCDYA ILVGKRRSIP
IIEGLKEENY KEDRIIVVNS LDEATKVLSK IVQFGDIVLF ENDLPDNYNE N
//
