(data stored in SCRATCH zone)

SWISSPROT: C5B764_EDWI9

ID   C5B764_EDWI9            Unreviewed;       244 AA.
AC   C5B764;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000256|HAMAP-Rule:MF_00766};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00766};
DE   AltName: Full=Glycan polymerase {ECO:0000256|HAMAP-Rule:MF_00766};
DE   AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000256|HAMAP-Rule:MF_00766};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_00766};
GN   Name=mtgA {ECO:0000256|HAMAP-Rule:MF_00766};
GN   OrderedLocusNames=NT01EI_0610 {ECO:0000313|EMBL:ACR67838.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67838.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC       elongation from lipid-linked precursors. {ECO:0000256|HAMAP-
CC       Rule:MF_00766, ECO:0000256|SAAS:SAAS00698205}.
CC   -!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
CC       Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
CC       Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC       diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
CC       Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
CC       diphosphate. {ECO:0000256|HAMAP-Rule:MF_00766,
CC       ECO:0000256|SAAS:SAAS00698209}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00766, ECO:0000256|SAAS:SAAS00687732}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00766, ECO:0000256|SAAS:SAAS00698204}; Single-pass
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_00766,
CC       ECO:0000256|SAAS:SAAS00698204}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00766, ECO:0000256|SAAS:SAAS00687728}.
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DR   EMBL; CP001600; ACR67838.1; -; Genomic_DNA.
DR   RefSeq; WP_015870035.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0610; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; ACR67838; ACR67838; NT01EI_0610.
DR   GeneID; 7960377; -.
DR   KEGG; eic:NT01EI_0610; -.
DR   PATRIC; fig|634503.3.peg.553; -.
DR   eggNOG; ENOG4108VKV; Bacteria.
DR   eggNOG; COG0744; LUCA.
DR   HOGENOM; HOG000288117; -.
DR   KO; K03814; -.
DR   OMA; PAPKCFD; -.
DR   OrthoDB; POG091H03R6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; -; 1.
DR   HAMAP; MF_00766; Mono_pep_trsgly; 1.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom.
DR   InterPro; IPR011812; Pep_trsgly.
DR   Pfam; PF00912; Transgly; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   TIGRFAMs; TIGR02070; mono_pep_trsgly; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B764.
DR   SWISS-2DPAGE; C5B764.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00698202};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00643808};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00687730};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00687729};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00698208, ECO:0000313|EMBL:ACR67838.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00687734};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00687736};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00705467, ECO:0000313|EMBL:ACR67838.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00687733};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00687740}.
FT   TRANSMEM     21     43       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00766}.
FT   DOMAIN       64    230       Transgly. {ECO:0000259|Pfam:PF00912}.
SQ   SEQUENCE   244 AA;  27658 MW;  3FDD65DCE2DECC63 CRC64;
     MSQTAASRRV FQHLWCWGRR LVFALLGAWI AALLIFAVLP VPYSSVMVQR QIGAWLHGDF
     SYIAYQTWRP MSQIAPQMAL AAIAAEDQSF PQHWGFDLTA IGQALDSADE EGSPLRGAST
     LSQQTMKNLL LWDGRSWLRK GLEAPLTLAE ELVWSKRRIL TVYLNIAEFG PGVFGVEEAA
     QRYFHKSARR LTAGEAALLA AVLPNPHRFS VRAPSRYVLQ RQRWILRQMH QLGGEAFLQR
     YDLH
//

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