(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE1344

ID   ACAM1_1_PE1344                       STANDARD;      PRT;   499 AA.
AC   ACAM1_1_PE1344; B0C6L4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate--2,
DE   6-diaminopimelate ligase; (ACAM1_1.PE1344).
GN   Name=murE; OrderedLocusNames=AM1_1404;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1344.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0C6L4_ACAM1
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
CC   -!- GENE_FAMILY: HOG000268118 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0C6L4; -.
DR   EMBL; CP000828; ABW26435.1; -; Genomic_DNA.
DR   RefSeq; YP_001515749.1; NC_009925.1.
DR   ProteinModelPortal; B0C6L4; -.
DR   STRING; B0C6L4; -.
DR   GeneID; 5680225; -.
DR   GenomeReviews; CP000828_GR; AM1_1404.
DR   KEGG; amr:AM1_1404; -.
DR   OMA; IGTIANY; -.
DR   ProtClustDB; PRK00139; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00208; MurE; 1; -.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; Mur_ligase_C; 1.
DR   SUPFAM; SSF53623; Mur_ligase_cen; 1.
DR   TIGRFAMs; TIGR01085; MurE; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   HOGENOMDNA; ACAM1_1.PE1344; -.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
SQ   SEQUENCE   499 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGMVKLRTLL AELSTHLWET PPTDHPALDA EITGLTTNSW AVQPGYLFIG MPGTRVDGGS
     FWKSAIEAGA AAALVSDQVD RADVGTHCVL ALKDMPRACA EVAATFYDQP SQKLKLVGMT
     GTNGKTTTTH LIEYLLTTAQ APTALFGTLY ARWPGHQVTA AHTTPFAVDL QQQLSDAVAA
     QCQFGVMEVS SHALAQKRVL GCQFTVAVFS NLTQDHLDYH QDMEDYFAAK ALLFSPDYLQ
     GRAIINIDDV YGQRLVDQIG PNQCWTYSIE GPADLYTSGL SYETAGVKGQ LHTPKGTVEF
     FSSLVGQFNV SNLLAAVGAV LELGLTLEQI TPALAQFPGV PGRMQQITYS ADQDISVIVD
     YAHTPDSLEN LLKAARPFVK GQMACVFGCG GDRDRTKRPL MGEIAARLSD QAIVTSDNPR
     TEDPQQILQD VLAGIPMEVK PIVEVDRRVA IQAAIAQAKP GDTILIAGKG HEDYQILGTE
     KIHFDDREEA QAALAQRYG
//

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