ID   HBHA_MYCBP              Reviewed;         199 AA.
AC   A1KFU9; O85733; P0A5P7; Q11142;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Heparin-binding hemagglutinin;
DE   AltName: Full=Adhesin;
GN   Name=hbhA; OrderedLocusNames=BCG_0516;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 61-68; 75-81; 83-92
RP   AND 123-138, AND CHARACTERIZATION.
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=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-17, AND CHARACTERIZATION.
RX   PubMed=9064359; DOI=10.1084/jem.184.3.993;
RA   Menozzi F.D., Rouse J.H., Alavi M., Laude-Sharp M., Muller J., Bischoff R.,
RA   Brennan M.J., Locht C.;
RT   "Identification of a heparin-binding hemagglutinin present in
RT   Mycobacteria.";
RL   J. Exp. Med. 184:993-1001(1996).
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   -!- 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; AM408590; CAL70501.1; -; Genomic_DNA.
DR   RefSeq; WP_003402339.1; NC_008769.1.
DR   AlphaFoldDB; A1KFU9; -.
DR   SMR; A1KFU9; -.
DR   PRIDE; A1KFU9; -.
DR   GeneID; 45424436; -.
DR   KEGG; mbb:BCG_0516; -.
DR   HOGENOM; CLU_089817_1_0_11; -.
DR   OMA; RERWANL; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell adhesion; Direct protein sequencing; Glycoprotein; Hemagglutinin;
KW   Heparin-binding; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9064359"
FT   CHAIN           2..199
FT                   /note="Heparin-binding hemagglutinin"
FT                   /id="PRO_0000285179"
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"
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