OATA_STAA8
ID OATA_STAA8 Reviewed; 603 AA.
AC Q2FV54;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=O-acetyltransferase OatA {ECO:0000303|PubMed:32350117};
DE EC=2.3.1.- {ECO:0000269|PubMed:32350117};
GN Name=oatA {ECO:0000303|PubMed:32350117}; OrderedLocusNames=SAOUHSC_02885;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION.
RX PubMed=15661003; DOI=10.1111/j.1365-2958.2004.04446.x;
RA Bera A., Herbert S., Jakob A., Vollmer W., Goetz F.;
RT "Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan
RT O-acetyltransferase OatA is the major determinant for lysozyme resistance
RT of Staphylococcus aureus.";
RL Mol. Microbiol. 55:778-787(2005).
RN [3] {ECO:0007744|PDB:6VJP, ECO:0007744|PDB:6WN9}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 445-601 OF MUTANTS
RP 1-MET--LYS-444/ALA-495/ALA-496 AND 1-MET--LYS-444/ALA-551/ALA-552 IN
RP COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE,
RP MUTAGENESIS OF 1-MET--LYS-444; SER-453; ASP-457; LYS-464; LYS-465; VAL-475;
RP LYS-495; LYS-496; ASN-507; GLU-551; LYS-552; ASP-575 AND HIS-578, AND
RP REACTION MECHANISM.
RX PubMed=32350117; DOI=10.1074/jbc.ra120.013108;
RA Jones C.S., Sychantha D., Howell P.L., Clarke A.J.;
RT "Structural basis for the O-acetyltransferase function of the
RT extracytoplasmic domain of OatA from Staphylococcus aureus.";
RL J. Biol. Chem. 295:8204-8213(2020).
CC -!- FUNCTION: Responsible for O-acetylation at the C(6)-hydroxyl group of
CC N-acetylmuramyl residues, forming the corresponding N,6-O-
CC diacetylmuramic acid of the peptidoglycan (PubMed:15661003,
CC PubMed:32350117). O-acetylation of the peptidoglycan is the major
CC determinant for lysozyme resistance (PubMed:15661003).
CC {ECO:0000269|PubMed:15661003, ECO:0000269|PubMed:32350117}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:32350117}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR EMBL; CP000253; ABD31881.1; -; Genomic_DNA.
DR RefSeq; WP_000379821.1; NZ_LS483365.1.
DR RefSeq; YP_501338.1; NC_007795.1.
DR PDB; 6VJP; X-ray; 1.71 A; A/B=445-601.
DR PDB; 6WN9; X-ray; 1.55 A; A/B=445-601.
DR PDBsum; 6VJP; -.
DR PDBsum; 6WN9; -.
DR AlphaFoldDB; Q2FV54; -.
DR SMR; Q2FV54; -.
DR STRING; 1280.SAXN108_2818; -.
DR PRIDE; Q2FV54; -.
DR EnsemblBacteria; ABD31881; ABD31881; SAOUHSC_02885.
DR GeneID; 3921554; -.
DR KEGG; sao:SAOUHSC_02885; -.
DR PATRIC; fig|93061.5.peg.2607; -.
DR eggNOG; COG1835; Bacteria.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_005679_11_2_9; -.
DR OMA; NRWLTNP; -.
DR PRO; PR:Q2FV54; -.
DR Proteomes; UP000008816; Chromosome.
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 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 3D-structure; Acyltransferase; Cell membrane; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..603
FT /note="O-acetyltransferase OatA"
FT /id="PRO_0000289545"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 453
FT /evidence="ECO:0000269|PubMed:32350117"
FT ACT_SITE 575
FT /evidence="ECO:0000269|PubMed:32350117"
FT ACT_SITE 578
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 1..444
FT /note="Missing: Has esterase and transferase activity using
FT 4-methylumbelliferyl acetate (4MU-Ac) and pentaacetyl-
FT chitopentaose as substrates, respectively."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 453
FT /note="S->A: Loss of esterase activity using 4-
FT methylumbelliferyl acetate (4MU-Ac) as substrate; when
FT associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 457
FT /note="D->A: 292% increased relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate
FT and 766% increased relative transferase activity with
FT pentaacetyl-chitopentaose as substrate; when associated
FT with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 457
FT /note="D->N: 285% increased relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate
FT and 562% increased relative transferase activity with
FT pentaacetyl-chitopentaose as substrate; when associated
FT with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 464..465
FT /note="KK->AA: 6% increased relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate;
FT when associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 475
FT /note="V->G: Loss of esterase activity using 4-
FT methylumbelliferyl acetate (4MU-Ac) as substrate; when
FT associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 495..496
FT /note="KK->AA: 14% increased relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate;
FT when associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 507
FT /note="N->A: Loss of esterase activity using 4-
FT methylumbelliferyl acetate (4MU-Ac) as substrate; when
FT associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 551..552
FT /note="EK->AA: 15% increased relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate;
FT when associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 575
FT /note="D->A: 1.02% residual relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate;
FT when associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT MUTAGEN 578
FT /note="H->A: 2.08% residual relative esterase activity
FT using 4-methylumbelliferyl acetate (4MU-Ac) as substrate;
FT when associated with 1-M--K-444."
FT /evidence="ECO:0000269|PubMed:32350117"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:6WN9"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 479..489
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:6WN9"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:6WN9"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:6WN9"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 539..552
FT /evidence="ECO:0007829|PDB:6WN9"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:6WN9"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:6WN9"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:6WN9"
FT HELIX 581..597
FT /evidence="ECO:0007829|PDB:6WN9"
SQ SEQUENCE 603 AA; 69099 MW; B9050E0DE20B8DF1 CRC64;
MDTKDFKRLE KMYSPRYLPG LDGLRAFAVI GIIIYHLNAQ WLSGGFLGVD TFFVISGYLI
TSLLISEYYR TQKIDLLEFW KRRLKRLIPA VLFLICVVLT FTLIFKPELI IQMKRDAIAA
IFYVSNWWYI SQNVDYFNQF AIEPLKHLWS LAIEEQFYLL FPLVITFLLH RFKPRNIIQT
LFIVSLISLG LMIVIHFITG DNSRVYFGTD TRLQTLLLGC ILAFIWPPFA LKKDISKKIV
VSLDIIGISG FAVLMTLFFI VGDQDQWIYN GGFYIISFAT LFIIAIAVHP SSLFAKFLSM
KPLLIIGKRS YSLYLWHYPI IVFVNSYYVQ GQIPVYVYII EILLTALMAE ISYRFIETPI
RKKGFKAFAF LPKKKGQFAR TVLVILLLVP SIVVLSGQFD ALGKQHEAEK KEKKTEFKTT
KKKVVKKDKQ EDKQTANSKE DIKKSSPLLI GDSVMVDIGN VFTKKIPNAQ IDGKVGRQLV
DATPIVKSQY KDYAKKGQKV VVELGTNGAF TKDQLNELLD SFGKADIYLV SIRVPRDYEG
RINKLIYEAA EKRSNVHLVD WYKASAGHPE YFAYDGIHLE YAGSKALTDL IVKTMETHAT
NKK
