NHHA_NEIMB
ID NHHA_NEIMB Reviewed; 591 AA.
AC Q7DDJ2; Q9AQF0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Autotransporter adhesin NhhA {ECO:0000305};
DE AltName: Full=Neisseria hia homolog {ECO:0000303|PubMed:10891657};
DE AltName: Full=Type 5 secretion system autotransporter NhhA {ECO:0000305};
DE Flags: Precursor;
GN Name=nhhA {ECO:0000303|PubMed:10891657};
GN Synonyms=GNA0992 {ECO:0000303|PubMed:16803596},
GN hsf {ECO:0000312|EMBL:AAF41395.1};
GN OrderedLocusNames=NMB0992 {ECO:0000312|EMBL:AAF41395.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10891657; DOI=10.1111/j.1574-695x.2000.tb01494.x;
RA Peak I.R., Srikhanta Y., Dieckelmann M., Moxon E.R., Jennings M.P.;
RT "Identification and characterisation of a novel conserved outer membrane
RT protein from Neisseria meningitidis.";
RL FEMS Immunol. Med. Microbiol. 28:329-334(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=MC58;
RX PubMed=16803596; DOI=10.1111/j.1365-2958.2006.05261.x;
RA Scarselli M., Serruto D., Montanari P., Capecchi B., Adu-Bobie J.,
RA Veggi D., Rappuoli R., Pizza M., Arico B.;
RT "Neisseria meningitidis NhhA is a multifunctional trimeric autotransporter
RT adhesin.";
RL Mol. Microbiol. 61:631-644(2006).
CC -!- FUNCTION: Involved in adhesion of capsulated meningococci to host
CC epithelial cells. Interacts with laminin and heparan sulfate, promoting
CC the adherence to the extracellular matrix (ECM) components.
CC {ECO:0000269|PubMed:16803596}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16803596}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16803596}. Cell
CC outer membrane {ECO:0000269|PubMed:16803596}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface. {ECO:0000269|PubMed:16803596}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface. {ECO:0000269|PubMed:16803596}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene decreases the ability to
CC adhere to Chang epithelial cells. {ECO:0000269|PubMed:16803596}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; AF125375; AAK09243.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41395.1; -; Genomic_DNA.
DR RefSeq; NP_274028.1; NC_003112.2.
DR RefSeq; WP_002222588.1; NC_003112.2.
DR AlphaFoldDB; Q7DDJ2; -.
DR SMR; Q7DDJ2; -.
DR STRING; 122586.NMB0992; -.
DR PaxDb; Q7DDJ2; -.
DR EnsemblBacteria; AAF41395; AAF41395; NMB0992.
DR KEGG; nme:NMB0992; -.
DR PATRIC; fig|122586.8.peg.1257; -.
DR HOGENOM; CLU_541568_0_0_4; -.
DR OMA; DSNWAVY; -.
DR Proteomes; UP000000425; Chromosome.
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 GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1780.10; -; 1.
DR InterPro; IPR008635; Coiled_stalk_dom.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR028230; TAA-Trp-ring.
DR InterPro; IPR037174; Trimeric_adhesin.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF13018; ESPR; 1.
DR Pfam; PF15401; TAA-Trp-ring; 1.
DR Pfam; PF03895; YadA_anchor; 1.
DR Pfam; PF05662; YadA_stalk; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport; Virulence.
FT SIGNAL 1..51
FT /evidence="ECO:0000255"
FT CHAIN 52..591
FT /note="Autotransporter adhesin NhhA"
FT /id="PRO_5004287540"
FT TRANSMEM 537..547
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 551..561
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 570..576
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 580..591
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 52..503
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305|PubMed:16803596"
FT REGION 504..591
FT /note="Translocator domain"
FT /evidence="ECO:0000305|PubMed:16803596"
FT CONFLICT 55..58
FT /note="EQEE -> RPRKK (in Ref. 1; AAK09243)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> V (in Ref. 1; AAK09243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 62112 MW; 7C22F3CAE7F73EC6 CRC64;
MNKIYRIIWN SALNAWVVVS ELTRNHTKRA SATVKTAVLA TLLFATVQAS ANNEEQEEDL
YLDPVQRTVA VLIVNSDKEG TGEKEKVEEN SDWAVYFNEK GVLTAREITL KAGDNLKIKQ
NGTNFTYSLK KDLTDLTSVG TEKLSFSANG NKVNITSDTK GLNFAKETAG TNGDTTVHLN
GIGSTLTDTL LNTGATTNVT NDNVTDDEKK RAASVKDVLN AGWNIKGVKP GTTASDNVDF
VRTYDTVEFL SADTKTTTVN VESKDNGKKT EVKIGAKTSV IKEKDGKLVT GKDKGENGSS
TDEGEGLVTA KEVIDAVNKA GWRMKTTTAN GQTGQADKFE TVTSGTNVTF ASGKGTTATV
SKDDQGNITV MYDVNVGDAL NVNQLQNSGW NLDSKAVAGS SGKVISGNVS PSKGKMDETV
NINAGNNIEI TRNGKNIDIA TSMTPQFSSV SLGAGADAPT LSVDGDALNV GSKKDNKPVR
ITNVAPGVKE GDVTNVAQLK GVAQNLNNRI DNVDGNARAG IAQAIATAGL VQAYLPGKSM
MAIGGGTYRG EAGYAIGYSS ISDGGNWIIK GTASGNSRGH FGASASVGYQ W
