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Database: UniProt
Entry: A0A239KYQ2_9SPHN
LinkDB: A0A239KYQ2_9SPHN
Original site: A0A239KYQ2_9SPHN 
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.
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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
//
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