ID   B3T7B6_9ZZZZ            Unreviewed;       480 AA.
AC   B3T7B6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative Mur ligase family, catalytic domain protein {ECO:0000313|EMBL:ABZ08475.1};
GN   ORFNames=ALOHA_HF4000APKG3D20ctg1g23 {ECO:0000313|EMBL:ABZ08475.1};
OS   uncultured marine microorganism HF4000_APKG3D20.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=455549 {ECO:0000313|EMBL:ABZ08475.1};
RN   [1] {ECO:0000313|EMBL:ABZ08475.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA   Konstantinidis K.T., Delong E.F.;
RT   "Genomic patterns of recombination, clonal divergence and environment in
RT   marine microbial populations.";
RL   ISME J. 2:1052-1065(2008).
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DR   EMBL; EU016629; ABZ08475.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3T7B6; -.
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   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; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABZ08475.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          5..99
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          110..294
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          329..411
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   480 AA;  52525 MW;  450FA794D9E6D23A CRC64;
     MRVFFIGICG TAMGNAAVLL KRQGFEVAGS DAGVYPPMSD VLADADIEFF EGFEEEALSN
     WSADRVVVGN AVSRGNPQVE WLLRERSVPF VCLPQLIGEE LIGRRPTVVV AGTHGKTTTT
     SLTAFALCEA GCNPGYLVGG VPLDLPSGSE LGDSEAPFVI EGDEYDSAFF DKRSKFIHYR
     PRILILNNLE FDHSDIFRDL ADVSRSFDNL LRIVPSDGYV LLNGDDTNLF DLPDAPWTTM
     LSVGTGEKND LCITGFSEGP TGASFKLVWR GCEVGEIDWH LPGEYNARNV AMAALGSALA
     QAVSSGDEPS LDNPFAALGL PPFDKCRGVK RRQEILVERE GLVVLSDFAH HPTAIAGALV
     SMRARWPEHR IIACFEPRSN TAVTNVFQDE FTEALAQADE VLIGAIHRAE RFADNERLDA
     DAMVQRFREK GLAGKAFSTN EALGEFLDEE EFKPEKKVLV AFFSNGSFDG VIDQVAERFR
//