ID A0A239KYQ2_9SPHN Unreviewed; 460 AA.
AC A0A239KYQ2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:SNT23496.1};
GN ORFNames=SAMN06295955_1181 {ECO:0000313|EMBL:SNT23496.1};
OS Sphingopyxis indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=436663 {ECO:0000313|EMBL:SNT23496.1, ECO:0000313|Proteomes:UP000198339};
RN [1] {ECO:0000313|EMBL:SNT23496.1, ECO:0000313|Proteomes:UP000198339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS15 {ECO:0000313|EMBL:SNT23496.1,
RC ECO:0000313|Proteomes:UP000198339};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FZPA01000018; SNT23496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239KYQ2; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000198339; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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 InterPro; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SNT23496.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000198339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..105
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 114..289
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 310..364
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 460 AA; 47796 MW; D70B9836A022D2D1 CRC64;
MAENKSYFFC GIGGSGMLPL AMIVAARGAH VAGSDRSRDQ GRSADKFDWI AGRGIALFPQ
DGSGLAAGQT LVASAAVEDS VPDVAAANAL GLPRMTRADL NAALFNEAAQ AIGVGGTSGK
STVTGMIGWI LESAGRRPTV MNGAVMRNFA NADRPFASAL IGDRSTYVSE VDESDGSIAL
YRPDVAVVTN ISLDHKSLDE LHALFGDFAA KARIAVINAD DPESAPLLAG GNVIRFGFSN
AAAVRGSDFE PMPDGCRFVV HFAGDRHAVR LRMPGRHNAM NALASIAAAR AVNVPVAQSV
AALAGFTGLA RRYEVLGQAG GVTVIDDFAH NPDKVAATLA AVAELPGRAL LFFQPHGYGP
LRQMGKELAA SFARGMRADD RLYVCDPVYF GGTVDRSIGS EALVADIVGS GGDAVHLTTR
AACGAAMLEE AQPGDRILIL GARDDTLTEF GRDLLVRLGG
//