ID   K1YNC1_9BACT            Unreviewed;       464 AA.
AC   K1YNC1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACD_79C00972G0015 {ECO:0000313|EMBL:EKD26909.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD26909.1};
RN   [1] {ECO:0000313|EMBL:EKD26909.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD26909.1}.
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DR   EMBL; AMFJ01035441; EKD26909.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1YNC1; -.
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: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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..112
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          120..292
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   464 AA;  51610 MW;  6C7E06DC629F98B4 CRC64;
     MMNIFKEKKY KNILVLGAGG SGMNVVCQYL VSNGIIVYAS DRGFDQDKKT RIKNILSSKG
     VKIINEKNNI SDKKIDFLII TPAVENEHNS ILQAKELGIP VIKRTEFLLD IFNSSNGIAI
     AGTSGKTTIT GMTATVLHKN NLNYTTICGD EILNFSDDSN LGNFIPGDRD KILLELDESD
     GSLPLYKPGI ASLSTLEKDH YKLSELESMF NVFCGNTKKI IINIDNPNLF KFYTSYKSKC
     VSVSTLNKNA DLFGEITEVS GNRIYFHING KKGVLNISGM YNVNNALCAA AVSGEAGVSL
     DKSLESLSYF KGVRNRFETL EIDNKFIILD FAHNPEKIKA SLISAQNLSK PVTYIFQPHG
     YGPLKFMLDE FASAFNDCLR TQDTLILLKV FDAGGTADRT IQSNNLLEKI NHDNVLYIED
     KNELNVYFKK NNSKSITWVI AGARDESLRD IQKEFYKIAQ GNIG
//