ID   HBHA_MYCTO              Reviewed;         199 AA.
AC   P9WIP8; L0T5H0; O85733; P0A5P6; Q11142;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Heparin-binding hemagglutinin;
DE   AltName: Full=Adhesin;
GN   Name=hbhA; OrderedLocusNames=MT0493;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: To M.leprae HbhA. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44716.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK44716.1; ALT_INIT; Genomic_DNA.
DR   PIR; F70742; F70742.
DR   RefSeq; WP_003402339.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIP8; -.
DR   SMR; P9WIP8; -.
DR   EnsemblBacteria; AAK44716; AAK44716; MT0493.
DR   GeneID; 45424436; -.
DR   KEGG; mtc:MT0493; -.
DR   PATRIC; fig|83331.31.peg.522; -.
DR   HOGENOM; CLU_089817_1_0_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   Cell adhesion; Glycoprotein; Hemagglutinin; Heparin-binding; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..199
FT                   /note="Heparin-binding hemagglutinin"
FT                   /id="PRO_0000427967"
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