ID   PERB_ECO57              Reviewed;         221 AA.
AC   Q7DBF7; Q7ACQ5;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=GDP-perosamine N-acetyltransferase {ECO:0000303|PubMed:18201574};
DE            EC=2.3.1.227 {ECO:0000269|PubMed:18201574};
GN   Name=perB {ECO:0000303|PubMed:18201574};
GN   Synonyms=wbdR {ECO:0000312|EMBL:AAG57089.1};
GN   OrderedLocusNames=ECs2831 {ECO:0000312|EMBL:BAB36254.1},
GN   Z3192 {ECO:0000312|EMBL:AAG57089.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   SUBUNIT.
RC   STRAIN=O157:H7 / EHEC;
RX   PubMed=18201574; DOI=10.1016/j.febslet.2008.01.005;
RA   Albermann C., Beuttler H.;
RT   "Identification of the GDP-N-acetyl-d-perosamine producing enzymes from
RT   Escherichia coli O157:H7.";
RL   FEBS Lett. 582:479-484(2008).
CC   -!- FUNCTION: Catalyzes the transfer of an acetyl residue from acetyl-CoA
CC       onto GDP-perosamine to form GDP-N-acetyl-perosamine.
CC       {ECO:0000269|PubMed:18201574}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + GDP-alpha-D-perosamine = CoA + GDP-N-acetyl-
CC         alpha-D-perosamine + H(+); Xref=Rhea:RHEA:36811, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:73996,
CC         ChEBI:CHEBI:73997; EC=2.3.1.227;
CC         Evidence={ECO:0000269|PubMed:18201574};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.32 mM for GDP-perosamine {ECO:0000269|PubMed:18201574};
CC         KM=1.8 mM for acetyl-CoA {ECO:0000269|PubMed:18201574};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:18201574};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000303|PubMed:18201574}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18201574}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005174; AAG57089.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36254.1; -; Genomic_DNA.
DR   RefSeq; NP_310858.1; NC_002695.1.
DR   RefSeq; WP_001055391.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q7DBF7; -.
DR   SMR; Q7DBF7; -.
DR   STRING; 386585.gene:10365872; -.
DR   EnsemblBacteria; AAG57089; AAG57089; Z3192.
DR   EnsemblBacteria; BAB36254; BAB36254; ECs_2831.
DR   GeneID; 912352; -.
DR   KEGG; ece:Z3192; -.
DR   KEGG; ecs:ECs_2831; -.
DR   PATRIC; fig|83334.175.peg.946; -.
DR   HOGENOM; CLU_081811_1_1_6; -.
DR   OMA; GAHCIIN; -.
DR   BioCyc; MetaCyc:MON-21546; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03360; LbH_AT_putative; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR041561; PglD_N.
DR   InterPro; IPR020019; Sia_OAcTrfase_NeuD-like.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 2.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF17836; PglD_N; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR03570; NeuD_NnaD; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Lipopolysaccharide biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..221
FT                   /note="GDP-perosamine N-acetyltransferase"
FT                   /id="PRO_0000430722"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P9D1"
SQ   SEQUENCE   221 AA;  23742 MW;  261157C480FE080C CRC64;
     MNLYGIFGAG SYGRETIPIL NQQIKQECGS DYALVFVDDV LAGKKVNGFE VLSTNCFLKA
     PYLKKYFNVA IANDKIRQRV SESILLHGVE PITIKHPNSV VYDHTMIGSG AIISPFVTIS
     TNTHIGRFFH ANIYSYVAHD CQIGDYVTFA PGAKCNGYVV IEDNAYIGSG AVIKQGVPNR
     PLIIGAGAII GMGAVVTKSV PAGITVCGNP AREMKRSPTS I