HBHA_MYCTU
ID HBHA_MYCTU Reviewed; 199 AA.
AC P9WIP9; L0T5H0; O85733; P0A5P6; Q11142;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Heparin-binding hemagglutinin;
DE AltName: Full=Adhesin;
GN Name=hbhA; OrderedLocusNames=Rv0475; ORFNames=MTCY20G9.01;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9770536; DOI=10.1073/pnas.95.21.12625;
RA Menozzi F.D., Bischoff R., Fort E., Brennan M.J., Locht C.;
RT "Molecular characterization of the mycobacterial heparin-binding
RT hemagglutinin, a mycobacterial adhesin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12625-12630(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP FUNCTION.
RC STRAIN=103;
RX PubMed=11449276; DOI=10.1038/35084083;
RA Pethe K., Alonso S., Biet F., Delogu G., Brennan M.J., Locht C.,
RA Menozzi F.D.;
RT "The heparin-binding haemagglutinin of M. tuberculosis is required for
RT extrapulmonary dissemination.";
RL Nature 412:190-194(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Required for extrapulmonary dissemination. Mediates adherence
CC to epithelial cells by binding to sulfated glycoconjugates present at
CC the surface of these cells; binds heparin, dextran sulfate, fucoidan
CC and chondroitin sulfate. Promotes hemagglutination of erythrocytes of
CC certain host species. Induces mycobacterial aggregation.
CC {ECO:0000269|PubMed:11449276}.
CC -!- INTERACTION:
CC P9WIP9; P9WIP9: hbhA; NbExp=4; IntAct=EBI-6414030, EBI-6414030;
CC -!- SUBCELLULAR LOCATION: Cell surface.
CC -!- DOMAIN: Heparin binding seems to require the C-terminal domain of HbhA.
CC Progressive truncations from the C-terminal end diminish the affinity
CC for heparin.
CC -!- PTM: Glycosylated. Glycosylation may protect the protein from
CC proteolytic degradation and be important for hemagglutination. It
CC suggests that the carbohydrate moiety may be located within the C-
CC terminal domain of HbhA.
CC -!- MISCELLANEOUS: Serum from patients diagnosed with active tuberculosis
CC that had not been vaccinated contains antibodies that recognize HbhA,
CC whereas serum from healthy individuals does not contain any.
CC -!- SIMILARITY: To M.leprae HbhA. {ECO:0000305}.
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DR EMBL; AF074390; AAC26052.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43209.1; -; Genomic_DNA.
DR PIR; F70742; F70742.
DR RefSeq; NP_214989.1; NC_000962.3.
DR RefSeq; WP_003402339.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P9WIP9; -.
DR SMR; P9WIP9; -.
DR STRING; 83332.Rv0475; -.
DR PaxDb; P9WIP9; -.
DR DNASU; 886272; -.
DR GeneID; 45424436; -.
DR GeneID; 886272; -.
DR KEGG; mtu:Rv0475; -.
DR TubercuList; Rv0475; -.
DR eggNOG; ENOG50335M1; Bacteria.
DR OMA; RERWANL; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:MTBBASE.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008201; F:heparin binding; IDA:MTBBASE.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MTBBASE.
DR GO; GO:0044078; P:positive regulation by symbiont of host receptor-mediated endocytosis; IDA:MTBBASE.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Glycoprotein; Hemagglutinin;
KW Heparin-binding; Reference proteome; Virulence.
FT CHAIN 1..199
FT /note="Heparin-binding hemagglutinin"
FT /id="PRO_0000083910"
FT REGION 162..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 121
FT /note="R -> P (in Ref. 1; AAC26052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 21534 MW; E9C1C011F8B460ED CRC64;
MAENSNIDDI KAPLLAALGA ADLALATVNE LITNLRERAE ETRTDTRSRV EESRARLTKL
QEDLPEQLTE LREKFTAEEL RKAAEGYLEA ATSRYNELVE RGEAALERLR SQQSFEEVSA
RAEGYVDQAV ELTQEALGTV ASQTRAVGER AAKLVGIELP KKAAPAKKAA PAKKAAPAKK
AAAKKAPAKK AAAKKVTQK
