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Database: UniProt
Entry: A0A067EQ89_CITSI
LinkDB: A0A067EQ89_CITSI
Original site: A0A067EQ89_CITSI 
ID   A0A067EQ89_CITSI        Unreviewed;       363 AA.
AC   A0A067EQ89;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
GN   ORFNames=CISIN_1g0154212mg {ECO:0000313|EMBL:KDO57248.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO57248.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO57248.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KK784964; KDO57247.1; -; Genomic_DNA.
DR   EMBL; KK784964; KDO57248.1; -; Genomic_DNA.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_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; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..363
FT                   /note="Mur ligase central domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007371363"
FT   DOMAIN          48..231
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   363 AA;  40161 MW;  D7FB9CF50DF9C4CC CRC64;
     MWMLWLFLLE FQLKATGLAC LLQSGKRVMS ELDFAAQVIP RSIKILAVTG TNGKSTVVTF
     VGQMLNHLGI EAFVGGNLGN PLSEAAFHCI ALPSSKPKFQ VAVVEVSSYQ MEIPNKYFCP
     TVSVVLNLTP DHLERHKTMK NYALTKCHLF SHMVNTKLGL LPFGNQHLNE AIKGHRFNLA
     WIGAFPGVKI DTEAKTASFE VPAVGVVSQL QLHNMKVMGR HNYHNAAVAA LSVLGLDIGV
     DVEALNSTIE ILRTPPHRMQ IVHRDIQGVT WVDDSKATNL EATCTGLMDL KGHKCVILLG
     GQAKVLNGQE SNGFEKLIEP LNHHRCVITV CALLFLKIVI QFPKKEFSLP FSFFLFSFCV
     DHH
//
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