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Database: UniProt
Entry: E3GXW1_METFV
LinkDB: E3GXW1_METFV
Original site: E3GXW1_METFV 
ID   E3GXW1_METFV            Unreviewed;       406 AA.
AC   E3GXW1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Mur ligase middle domain protein {ECO:0000313|EMBL:ADP77143.1};
GN   OrderedLocusNames=Mfer_0340 {ECO:0000313|EMBL:ADP77143.1};
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP77143.1, ECO:0000313|Proteomes:UP000002315};
RN   [1] {ECO:0000313|EMBL:ADP77143.1, ECO:0000313|Proteomes:UP000002315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC   {ECO:0000313|Proteomes:UP000002315};
RX   PubMed=21304736;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
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DR   EMBL; CP002278; ADP77143.1; -; Genomic_DNA.
DR   RefSeq; WP_013413421.1; NC_014658.1.
DR   AlphaFoldDB; E3GXW1; -.
DR   STRING; 523846.Mfer_0340; -.
DR   GeneID; 9962055; -.
DR   KEGG; mfv:Mfer_0340; -.
DR   HOGENOM; CLU_629483_0_0_2; -.
DR   OrthoDB; 76119at2157; -.
DR   Proteomes; UP000002315; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADP77143.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002315}.
FT   DOMAIN          99..220
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   406 AA;  46344 MW;  23A2E25D1EA952A1 CRC64;
     MDTKKVAVLG LGVEGKNAIK SLKKRGYRIY ASDKNRIDFK DEEVEVDLGK HDINKILSCD
     FVVISPSMWN TKLASLIKKK KKVICDVFNK HKSIYTIGVT GTNGKTTTSL MIYEILKNSK
     KNVLIGGNAG GGFEGYTELI LEANEGNYEY MVIEICDMTL DFVDDCFDLD MVVVTNIGED
     HLNYHKTLEN FRRKLKKFLK NKIAILNSKD PNLVKLAKEL DNYIFYDEYD VPLFGRFNKL
     NAGAAAAAAK FLGIDPKIIS HTLKNFKLPK GRLKHYNINN KHIIIGKTDN KTALEAVLNE
     MKFDAMFIGT PRRNEYWRFK ILDVAYKSSP KLIVLFPGLE DTVDMAKKRL EKLGFKNVVT
     VKTIDEIVKM FEFVLEKYEK IFIGGNGQKK INKIQDILEA KFVQYQ
//
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