ID A0A1F8LNJ4_9CHLR Unreviewed; 403 AA.
AC A0A1F8LNJ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DUF1727 domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A2X23_02565 {ECO:0000313|EMBL:OGN87954.1};
OS Chloroflexi bacterium GWC2_73_18.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797616 {ECO:0000313|EMBL:OGN87954.1, ECO:0000313|Proteomes:UP000176763};
RN [1] {ECO:0000313|EMBL:OGN87954.1, ECO:0000313|Proteomes:UP000176763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN87954.1}.
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DR EMBL; MGMJ01000020; OGN87954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8LNJ4; -.
DR STRING; 1797616.A2X23_02565; -.
DR Proteomes; UP000176763; Unassembled WGS sequence.
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; 3.40.1190.10; Mur-like, catalytic 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; IPR013564; MurT_C.
DR PANTHER; PTHR23135:SF7; LIPID II ISOGLUTAMINYL SYNTHASE (GLUTAMINE-HYDROLYZING) SUBUNIT MURT; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF08353; MurT_C; 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;
FT DOMAIN 1..138
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 274..382
FT /note="Lipid II isoglutaminyl synthase (glutamine-
FT hydrolyzing) subunit MurT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08353"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGN87954.1"
SQ SEQUENCE 403 AA; 42900 MW; E4FD6780EBD5E595 CRC64;
GSNGKTTTAR LTAALLRGEG VAVSHNSAGA NLVQGVTSLA IGFADLRGRL PEGALVVEVD
EAALRVVAPE LDLRALLVTD LFRDQLDRYG EIYAVAGAIE KAAAGLPPDA SLVVNGDDPM
VAGLGLDREG RRVTFGFDLP GSTDRISRAA DTIRCPRCRA DLAYRHVYLS HMGEWRCPSC
GLVRPPLDVA VTSVEVVDLR ETRCTLQTPD GPLDLRIPQA GIHIAYDAAG AVAIAVGLGL
PIPHAAASLA TVGPAFGRLE TIAADGRRIV LGFAKNPTSF NTTLRALATE GEPRQLLVAA
SNTLVDGEDF AWLWDVDFEG AAGRVERVTV SGLRADELAN RLKYAGVDPA RMAIVTDRRA
ALDRALLDVK QGGTLVILAG YTPTIELREE MRKRGWVGRF WEA
//
