OATA_LISMO
ID OATA_LISMO Reviewed; 622 AA.
AC Q8Y7I6;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Peptidoglycan O-acetyltransferase OatA {ECO:0000303|PubMed:21844299};
DE EC=2.3.1.- {ECO:0000305|PubMed:21844299};
GN Name=oatA {ECO:0000303|PubMed:21844299};
GN OrderedLocusNames=lmo1291 {ECO:0000303|PubMed:21844299,
GN ECO:0000312|EMBL:CAC99369.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963 {ECO:0000312|EMBL:CAC99369.1};
RN [1] {ECO:0000312|EMBL:CAC99369.1, ECO:0000312|Proteomes:UP000000817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000312|Proteomes:UP000000817};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000303|PubMed:21844299};
RX PubMed=21844299; DOI=10.1093/infdis/jir396;
RA Aubry C., Goulard C., Nahori M.A., Cayet N., Decalf J., Sachse M.,
RA Boneca I.G., Cossart P., Dussurget O.;
RT "OatA, a peptidoglycan O-acetyltransferase involved in Listeria
RT monocytogenes immune escape, is critical for virulence.";
RL J. Infect. Dis. 204:731-740(2011).
CC -!- FUNCTION: Responsible for O-acetylation at the C6-hydroxyl group of N-
CC acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic
CC acid of the peptidoglycan. O-acetylation of the peptidoglycan is the
CC major determinant for lysozyme resistance. Critical for virulence and
CC escape from innate immune response of the host. Involved at both early
CC and later stages of listeriosis in the mouse model of infection.
CC Required for successful host colonization and for intracellular
CC survival of bacteria in macrophages of the infected host. Controls the
CC production of inflammatory mediators in the liver of the infected host.
CC Confers resistance to host antimicrobial molecules and to cell wall-
CC targeting molecules such as beta-lactam antibiotics and bacteriocins.
CC {ECO:0000269|PubMed:21844299}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Secreted, cell wall {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no O-acetylated N-
CC acetyl muramic acid residues on the cell wall. Sensitive to bacterial
CC cell wall targeting antimicrobial molecules lysozyme, beta-lactam
CC antibiotic cefotaxime and Staphylococcus gallinarum lantibiotic
CC gallidermin. Impaired postinfection intracellular survival of bacteria
CC inside human acute monocytic leukemia (THP-1) cells. Killed more
CC efficiently and rapidly in mouse postinfection peritoneal-elicited
CC macrophages (PEM) and bone marrow-derived macrophages (BMDM). Impaired
CC ability of the bacteria to multiply in infected murine macrophage-like
CC (RAW264.7) cells. Bacteria do not accumulate in vacuoles of the
CC infected RAW264.7 cells, but reside in the cytosol and the infected
CC cells are not forming protrusions. Virulence is drastically reduced in
CC mice following intravenous infection as observed by the dramatic
CC difference in LD(50) of the mutant (1100000 bacteria) compared to wild-
CC type (700 bacteria). With sublethal infectious doses, has a reduced
CC capacity to replicate in liver and spleen compared to wild-type. In the
CC intestinal lumen of intragastrically infected human E-cadherin
CC transgenic mice, which are permissive to Listeria oral infection, the
CC number of bacteria is strongly decreased 24 hours postinfection. There
CC are also significantly fewer bacteria in the small intestine tissue
CC compared to wild-type. Triggers increased secretion of cytokines
CC interleukin 2 (IL-2), IL-6, IL-12 and IL-5, and chemokines CCL2, CXCL9
CC and CCL3 from the liver cells of the infected mouse at 6 hours
CC postinfection. At later time points of infection, the production of the
CC inflammatory mediators is increased in case of IL-6, similar in case of
CC IL-2, CXCL9 and IL-5, and lower in case of IL-12, CCL2 and CCL3
CC compared to the wild-type. The virulence of a double oatA/pgdA deletion
CC mutant is more reduced than that of either single mutant as detected by
CC lack of colonization in the bloodstream, liver and spleen of infected
CC mouse 24 hours postinfection. {ECO:0000269|PubMed:21844299}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR EMBL; AL591978; CAC99369.1; -; Genomic_DNA.
DR PIR; AC1236; AC1236.
DR RefSeq; NP_464816.1; NC_003210.1.
DR RefSeq; WP_009932001.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y7I6; -.
DR SMR; Q8Y7I6; -.
DR STRING; 169963.lmo1291; -.
DR PaxDb; Q8Y7I6; -.
DR EnsemblBacteria; CAC99369; CAC99369; CAC99369.
DR GeneID; 985119; -.
DR KEGG; lmo:lmo1291; -.
DR PATRIC; fig|169963.11.peg.1326; -.
DR eggNOG; COG1835; Bacteria.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_005679_11_2_9; -.
DR OMA; NRWLTNP; -.
DR PhylomeDB; Q8Y7I6; -.
DR BioCyc; LMON169963:LMO1291-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic resistance; Cell membrane; Cell wall; Membrane;
KW Reference proteome; Secreted; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..622
FT /note="Peptidoglycan O-acetyltransferase OatA"
FT /id="PRO_0000452173"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 412..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 480
FT /evidence="ECO:0000250|UniProtKB:Q2FV54"
FT ACT_SITE 600
FT /evidence="ECO:0000250|UniProtKB:Q2FV54"
FT ACT_SITE 603
FT /evidence="ECO:0000250|UniProtKB:Q2FV54"
SQ SEQUENCE 622 AA; 70325 MW; 14A72E9BD2C825F5 CRC64;
MKRTTRYSRK YVPSIDGLRA LAVIAVIAYH LNFSWAKGGF IGVDIFFVLS GYLITNILLT
QWEKNQSLQL KQFWIRRFRR LIPAVYVMIV VVVIYSVFFH PEILKNLRGD AIASFFYVSN
WWFIFHNVSY FDSFGLPSPL KNLWSLAIEE QFYLIWPAFL LVFLKWVKNP KLLLKIVIGL
GLLSAVWMTI LYVPGTDPSR VYYGTDTRAF DLLSGCALAF VWPFNRLSPV VPRKSKAVLN
IAGTISILCF ILFTAFVSEY QPFLYRGGLL FVAILGVIMI ATISHPASYL SKIFSFKPLR
WIGTRSYGIY LWHYPIITLT TPVLEITQPN IWRAILQVAA TFIIAELSFR FIETPIRKNG
FINYFKGFKD KNYFIWKNKP VGKWLSIAGV VAVLAIFTLG MSNVLSVNTN AEKQQTSVKT
TTSTPDEKKD DKKEDKATKD KEADSNKASE QKETQKPDNK NKSAATPKTI ITQTVAIGDS
VMLDIEPYLK EAVPNITIDG LVGRQLRDAI TTATGYKKFN SENSSVILEL GTNGPFTEDQ
LNDLLDQFDK ATIYLVNTRV PRGWQSDVNK SIANAASRPN VTVVDWYSRS SGQSQYFAPD
GVHLTKAGAQ AYVAMLTSVM NK
