MNAA_BACSU
ID MNAA_BACSU Reviewed; 380 AA.
AC P39131;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase;
DE EC=5.1.3.14;
DE AltName: Full=UDP-GlcNAc-2-epimerase;
GN Name=mnaA; OrderedLocusNames=BSU35660;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8126437; DOI=10.1099/00221287-139-12-3185;
RA Soldo B., Lazarevic V., Margot P., Karamata D.;
RT "Sequencing and analysis of the divergon comprising gtaB, the structural
RT gene of UDP-glucose pyrophosphorylase of Bacillus subtilis 168.";
RL J. Gen. Microbiol. 139:3185-3195(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF THR-69 AND
RP PRO-374.
RX PubMed=12107153; DOI=10.1128/jb.184.15.4316-4320.2002;
RA Soldo B., Lazarevic V., Pooley H.M., Karamata D.;
RT "Characterization of a Bacillus subtilis thermosensitive teichoic acid-
RT deficient mutant: gene mnaA (yvyH) encodes the UDP-N-acetylglucosamine 2-
RT epimerase.";
RL J. Bacteriol. 184:4316-4320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the conversion of UDP-N-acetylglucosamine into UDP-
CC N-acetylmannosamine, a precursor of the teichoic acid linkage unit.
CC {ECO:0000269|PubMed:12107153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:68623; EC=5.1.3.14;
CC -!- PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000305}.
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DR EMBL; Z22516; CAA80240.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15583.1; -; Genomic_DNA.
DR PIR; D70049; D70049.
DR RefSeq; NP_391446.1; NC_000964.3.
DR RefSeq; WP_003243178.1; NZ_JNCM01000033.1.
DR PDB; 1O6C; X-ray; 2.90 A; A/B=2-380.
DR PDB; 4FKZ; X-ray; 1.69 A; A/B=1-380.
DR PDBsum; 1O6C; -.
DR PDBsum; 4FKZ; -.
DR AlphaFoldDB; P39131; -.
DR SMR; P39131; -.
DR STRING; 224308.BSU35660; -.
DR jPOST; P39131; -.
DR PaxDb; P39131; -.
DR PRIDE; P39131; -.
DR EnsemblBacteria; CAB15583; CAB15583; BSU_35660.
DR GeneID; 936209; -.
DR KEGG; bsu:BSU35660; -.
DR PATRIC; fig|224308.179.peg.3857; -.
DR eggNOG; COG0381; Bacteria.
DR InParanoid; P39131; -.
DR OMA; VYFVGDV; -.
DR PhylomeDB; P39131; -.
DR BioCyc; BSUB:BSU35660-MON; -.
DR BioCyc; MetaCyc:BSU35660-MON; -.
DR BRENDA; 5.1.3.14; 658.
DR UniPathway; UPA00827; -.
DR EvolutionaryTrace; P39131; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR029767; WecB-like.
DR PANTHER; PTHR43174; PTHR43174; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR TIGRFAMs; TIGR00236; wecB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Cytoplasm; Isomerase;
KW Reference proteome; Teichoic acid biosynthesis.
FT CHAIN 1..380
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000208532"
FT MUTAGEN 69
FT /note="T->I: In TS-21; temperature-sensitive, develops, at
FT the nonpermissive temperature (47 degrees Celsius), a
FT coccoid-like morphology, i.e. a phenotype associated with a
FT deficient synthesis of poly(glycerol phosphate) teichoic
FT acid."
FT /evidence="ECO:0000269|PubMed:12107153"
FT MUTAGEN 374
FT /note="P->L: In TS-21; temperature-sensitive, develops, at
FT the nonpermissive temperature (47 degrees Celsius), a
FT coccoid-like morphology, i.e. a phenotype associated with a
FT deficient synthesis of poly(glycerol phosphate) teichoic
FT acid."
FT /evidence="ECO:0000269|PubMed:12107153"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4FKZ"
FT TURN 128..133
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:4FKZ"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:4FKZ"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:4FKZ"
SQ SEQUENCE 380 AA; 42634 MW; 63A73C8D1E7D3B5A CRC64;
MKKLKVMTVF GTRPEAIKMA PLVLELKKYP EIDSYVTVTA QHRQMLDQVL DAFHIKPDFD
LNIMKERQTL AEITSNALVR LDELFKDIKP DIVLVHGDTT TTFAGSLAAF YHQIAVGHVE
AGLRTGNKYS PFPEELNRQM TGAIADLHFA PTGQAKDNLL KENKKADSIF VTGNTAIDAL
NTTVRDGYSH PVLDQVGEDK MILLTAHRRE NLGEPMENMF KAIRRIVGEF EDVQVVYPVH
LNPVVREAAH KHFGDSDRVH LIEPLEVIDF HNFAAKSHFI LTDSGGVQEE APSLGKPVLV
LRDTTERPEG VEAGTLKLAG TDEENIYQLA KQLLTDPDEY KKMSQASNPY GDGEASRRIV
EELLFHYGYR KEQPDSFTGK
