(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZKT9_PSEAB

ID   A0A0H2ZKT9_PSEAB        Unreviewed;       243 AA.
AC   A0A0H2ZKT9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 17.
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   ECO:0000313|EMBL:ABJ15344.1};
GN   OrderedLocusNames=PA14_04950 {ECO:0000313|EMBL:ABJ15344.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15344.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15344.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15344.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15344.1; -; Genomic_DNA.
DR   RefSeq; WP_003100972.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15344; ABJ15344; PA14_04950.
DR   KEGG; pau:PA14_04950; -.
DR   KO; K03814; -.
DR   OMA; PAPKCFD; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000653; 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; A0A0H2ZKT9.
DR   SWISS-2DPAGE; A0A0H2ZKT9.
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:UP000000653};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00698208};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_00766,
KW   ECO:0000256|SAAS:SAAS00705467};
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     20     41       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00766}.
FT   DOMAIN       65    229       Transgly. {ECO:0000259|Pfam:PF00912}.
SQ   SEQUENCE   243 AA;  27792 MW;  594634A2EA5CAA3C CRC64;
     MAAPFFQAKP RMLRSLFRRL FKYLLWFMAA SVVLVAVLRW VPPPGTMVMV ERKVGSWVDG
     QPIDLQRDWR SWEQLPDSLK VAVIAGEDQH FAEHHGFDLP AIQQALAHNE RGGSIRGAST
     LSQQVAKNVF LWSGRSWLRK GLEAWFTLLI ETLWTKQRIL EVYLNSAEWG PGVFGAQAAA
     RYHFGLDAER LSRTQASQLA AVLPSPLKWS AARPGPYVRQ RAAWIRQQMW QLGGDDYLLR
     LER
//

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