NADA5_NEIMI
ID NADA5_NEIMI Reviewed; 325 AA.
AC A0ELI2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Neisseria adhesin A {ECO:0000303|PubMed:25404323};
DE Short=NadA variant 5 {ECO:0000303|PubMed:25404323};
DE Flags: Precursor;
GN Name=nadA {ECO:0000303|Ref.1}; Synonyms=nadA5 {ECO:0000305};
OS Neisseria meningitidis serogroup B.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=491;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LNP15709;
RA Bambini S., Caugant D.A., Mora M., Santini L., Rappuoli R., Pizza M.,
RA Comanducci M.;
RT "NadA distribution and diversification in Neisseria meningitidis.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4CJD}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 24-221, SUBUNIT, AND DOMAIN.
RC STRAIN=M01-240320;
RX PubMed=25404323; DOI=10.1073/pnas.1419686111;
RA Malito E., Biancucci M., Faleri A., Ferlenghi I., Scarselli M., Maruggi G.,
RA Lo Surdo P., Veggi D., Liguori A., Santini L., Bertoldi I., Petracca R.,
RA Marchi S., Romagnoli G., Cartocci E., Vercellino I., Savino S.,
RA Spraggon G., Norais N., Pizza M., Rappuoli R., Masignani V.,
RA Bottomley M.J.;
RT "Structure of the meningococcal vaccine antigen NadA and epitope mapping of
RT a bactericidal antibody.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17128-17133(2014).
CC -!- FUNCTION: An antigenic bacterial cell surface protein that adheres to
CC and induces bacterial uptake by human epithelial cells.
CC {ECO:0000250|UniProtKB:P0DV44}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:25404323}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P0DV44}. Cell
CC outer membrane {ECO:0000250|UniProtKB:P0DV44}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Insertion of the C-
CC terminal translocator domain in the outer membrane forms a hydrophilic
CC pore for the translocation of the passenger domain to the bacterial
CC cell surface (By similarity). The head region (residues 27-137) forms
CC at the top of a long trimeric stalk. The head itself is almost
CC exclusively coiled-coil that can be divided in two fragments (residues
CC 34-48 and 85-137, respectively) separated by an insertion (residues 49-
CC 84) that forms 3 wing-like structures per trimer that pack against the
CC N-terminus. Only residues 27-137 and 199-210 gave a defined structure
CC (PubMed:25404323). {ECO:0000250|UniProtKB:P0C2W0,
CC ECO:0000269|PubMed:25404323, ECO:0007744|PDB:4CJD}.
CC -!- BIOTECHNOLOGY: Several alleles exist that vary in length, this is
CC allele 5, which is not cross-reactive with all antibodies against
CC alleles 1, 2, or 3. {ECO:0000269|PubMed:25404323}.
CC -!- MISCELLANEOUS: About 50% of hypervirulent serogroup B N.meningitidis
CC encode this protein. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
CC -!- CAUTION: The gene name nadA has also been given to quinolinate
CC synthase.
CC -!- WEB RESOURCE: Name=Bexsero meningococcal group B Vaccine;
CC URL="https://www.ema.europa.eu/en/medicines/human/EPAR/bexsero";
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DR EMBL; DQ239929; ABC25681.1; -; Genomic_DNA.
DR PDB; 4CJD; X-ray; 2.06 A; A=24-221.
DR PDBsum; 4CJD; -.
DR SMR; A0ELI2; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF03895; YadA_anchor; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Coiled coil; Membrane; Signal;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..325
FT /note="Neisseria adhesin A"
FT /evidence="ECO:0000255"
FT /id="PRO_5002624564"
FT TRANSMEM 270..280
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 284..295
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 302..308
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 314..325
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 24..137
FT /note="Head domain"
FT /evidence="ECO:0000269|PubMed:25404323"
FT REGION 139..231
FT /note="Coiled stalk domain"
FT /evidence="ECO:0000305|PubMed:25404323"
FT REGION 232..270
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 271..325
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT COILED 86..135
FT /evidence="ECO:0000305|PubMed:25404323,
FT ECO:0007744|PDB:4CJD"
SQ SEQUENCE 325 AA; 34124 MW; ABAEC8E01C13494C CRC64;
MKHFQSKVLT AAILAALSGS AMADNPPPST DEIAKAALVN SYNNTQDING FKVGDTIYDI
NGNGKITRKT ATEDDVKADD FGGLGLKEVL AQHDQSLADL TGTVDENSEA LVKTAEVVND
ISADVKANTA AIGENKAAIA KKADQTALDA VSEKVTANET AIGKKANSAD VYTKAEVYTK
QESDNRFVKI GDRIGNLNTT ANGLETRLAD AEKSVADHGT RLASAEKSIT EHGTRLNGLD
RTVSDLRKET RQGLAEQAAL SGLFQPYNVG RFNVTAAVGG YKSESAVAIG TGFRFTENFA
AKAGVAVGTS SGSSAAYHVG VNYEW
