BADA_BARHN
ID BADA_BARHN Reviewed; 3082 AA.
AC Q5MWV9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 23-FEB-2022, entry version 60.
DE RecName: Full=Autotransporter adhesin BadA {ECO:0000303|PubMed:21536788};
DE AltName: Full=Bartonella adhesin A {ECO:0000303|PubMed:15534369};
DE Short=BadA {ECO:0000303|PubMed:15534369};
DE AltName: Full=Non-fimbrial adhesin A {ECO:0000303|PubMed:15534369};
DE AltName: Full=Type 5 secretion system autotransporter BadA {ECO:0000305};
DE AltName: Full=Type IV pilus {ECO:0000303|PubMed:15534369};
DE Flags: Precursor;
GN Name=badA {ECO:0000303|PubMed:15534369};
OS Bartonella henselae (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=38323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Marseille;
RX PubMed=17060468; DOI=10.1128/iai.00963-06;
RA Riess T., Raddatz G., Linke D., Schafer A., Kempf V.A.;
RT "Analysis of Bartonella adhesin A expression reveals differences between
RT various B. henselae strains.";
RL Infect. Immun. 75:35-43(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-536 AND 2573-2761, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=Marseille;
RX PubMed=15534369; DOI=10.1084/jem.20040500;
RA Riess T., Andersson S.G., Lupas A., Schaller M., Schafer A., Kyme P.,
RA Martin J., Walzlein J.H., Ehehalt U., Lindroos H., Schirle M., Nordheim A.,
RA Autenrieth I.B., Kempf V.A.;
RT "Bartonella adhesin A mediates a proangiogenic host cell response.";
RL J. Exp. Med. 200:1267-1278(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=Marseille;
RX PubMed=18627378; DOI=10.1111/j.1462-5822.2008.01201.x;
RA Kaiser P.O., Riess T., Wagner C.L., Linke D., Lupas A.N., Schwarz H.,
RA Raddatz G., Schaefer A., Kempf V.A.;
RT "The head of Bartonella adhesin A is crucial for host cell interaction of
RT Bartonella henselae.";
RL Cell. Microbiol. 10:2223-2234(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Marseille;
RX PubMed=21536788; DOI=10.1128/iai.01309-10;
RA Mueller N.F., Kaiser P.O., Linke D., Schwarz H., Riess T., Schaefer A.,
RA Eble J.A., Kempf V.A.;
RT "Trimeric autotransporter adhesin-dependent adherence of Bartonella
RT henselae, Bartonella quintana, and Yersinia enterocolitica to matrix
RT components and endothelial cells under static and dynamic flow
RT conditions.";
RL Infect. Immun. 79:2544-2553(2011).
RN [5]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=Marseille;
RX PubMed=21981119; DOI=10.1111/j.1462-5822.2011.01711.x;
RA Kaiser P.O., Linke D., Schwarz H., Leo J.C., Kempf V.A.;
RT "Analysis of the BadA stalk from Bartonella henselae reveals domain-
RT specific and domain-overlapping functions in the host cell infection
RT process.";
RL Cell. Microbiol. 14:198-209(2012).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1, Marseille, and
RC various clinical strains;
RX PubMed=23163798; DOI=10.1111/cmi.12070;
RA Lu Y.Y., Franz B., Truttmann M.C., Riess T., Gay-Fraret J., Faustmann M.,
RA Kempf V.A., Dehio C.;
RT "Bartonella henselae trimeric autotransporter adhesin BadA expression
RT interferes with effector translocation by the VirB/D4 type IV secretion
RT system.";
RL Cell. Microbiol. 15:759-778(2013).
RN [7] {ECO:0007744|PDB:3D9X}
RP X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) OF 375-536, AND SUBUNIT.
RC STRAIN=Marseille;
RX PubMed=18688279; DOI=10.1371/journal.ppat.1000119;
RA Szczesny P., Linke D., Ursinus A., Bar K., Schwarz H., Riess T.M.,
RA Kempf V.A., Lupas A.N., Martin J., Zeth K.;
RT "Structure of the head of the Bartonella adhesin BadA.";
RL PLoS Pathog. 4:E1000119-E1000119(2008).
CC -!- FUNCTION: Mediates bacterial adherence to host endothelial cells and
CC host extracellular matrix proteins (collagen type I, III, IV, laminin
CC and fibronectin). Static versus dynamic adherence results differ
CC slightly; in dynamic adherence studies bacteria bind to fixed
CC components under a constant defined flow rate to simulate in vivo
CC infection conditions (PubMed:15534369, PubMed:17060468,
CC PubMed:18627378, PubMed:21536788, PubMed:23163798). Induces secretion
CC of host proangiogenic cytokines such as VEGFA, ADM, IGFBP-3 and IL-8.
CC May prevent bacterial phagocytosis by macrophages (PubMed:15534369)
CC (Probable). Probably mediates bacterial autoagglutination
CC (PubMed:17060468, PubMed:18627378). Negatively impacts type IV
CC secretion system effectors (VirB/D4 T4SS and its substrate Bep
CC proteins), possibly by preventing close association of host and
CC bacterial cells. This implies the 2 factors are expressed at different
CC times during infection (Probable). {ECO:0000269|PubMed:15534369,
CC ECO:0000269|PubMed:17060468, ECO:0000269|PubMed:18627378,
CC ECO:0000269|PubMed:21536788, ECO:0000269|PubMed:23163798,
CC ECO:0000305|PubMed:23163798}.
CC -!- SUBUNIT: Homotrimer (Probable). Crystals of the head region form
CC trimers (PubMed:18688279). {ECO:0000269|PubMed:18688279,
CC ECO:0000305|PubMed:18688279}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:15534369,
CC ECO:0000269|PubMed:18627378, ECO:0000269|PubMed:21536788,
CC ECO:0000269|PubMed:21981119, ECO:0000269|PubMed:23163798}. Cell outer
CC membrane {ECO:0000269|PubMed:15534369, ECO:0000269|PubMed:18627378}.
CC Note=Forms long (about 240 nm) filaments extending from the cell
CC surface, which were initially called type IV pili (PubMed:15534369,
CC PubMed:18627378, PubMed:21536788, PubMed:21981119, PubMed:23163798).
CC The C-terminal translocator domain is localized in the outer membrane
CC and the passenger domain is at the cell surface (By similarity).
CC {ECO:0000250|UniProtKB:P0C2W0, ECO:0000269|PubMed:15534369,
CC ECO:0000269|PubMed:18627378, ECO:0000269|PubMed:21536788,
CC ECO:0000269|PubMed:21981119, ECO:0000269|PubMed:23163798}.
CC -!- DOMAIN: The N-terminus (residues 48-376) performs most of the host-
CC associated functions of the protein and binds collagen. The large
CC central domain (composed of neck-stalk repeats about residue 470-2850)
CC is required to bind host fibronectin and contributes to host cell
CC adherence, collagen-binding and induction of host proangiogenic
CC factors. {ECO:0000269|PubMed:18627378, ECO:0000269|PubMed:21981119}.
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:0000250|UniProtKB:P0C2W0}.
CC -!- DISRUPTION PHENOTYPE: No longer binds to host cells or host
CC extracellular matrix proteins, loss of bacterial 'type IV-like pili'.
CC Bacteria are more frequently phagocytosed by murine J774 macrophages.
CC Infected HeLa cells no longer secrete proangiogenic factors such as
CC VEGFA, ADM, IGFBP3 or IL-8 (PubMed:15534369). Decreased binding to host
CC epithelial cells and to host extracellular matrix components
CC vitronectin, hyaluronate, fibronectin, laminin, collagens I, III and IV
CC under static and dynamic flow conditions (PubMed:21536788).
CC {ECO:0000269|PubMed:15534369, ECO:0000269|PubMed:21536788}.
CC -!- BIOTECHNOLOGY: Antisera to this protein are frequently present in
CC humans and animals infected by B.henselae, suggesting it might be
CC useful as a marker for B.henselae infection.
CC {ECO:0000305|PubMed:15534369}.
CC -!- MISCELLANEOUS: Infection with B.henselae leads to cat scratch disease
CC in immunocompetent individuals and bacillary angiomatosis, tumorous
CC proliferations of endothelial cells in the skin and internal organs in
CC immunocompromised patients. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; DQ665674; AAT69970.2; -; Genomic_DNA.
DR PDB; 3D9X; X-ray; 1.13 A; A/B/C=374-536.
DR PDBsum; 3D9X; -.
DR SMR; Q5MWV9; -.
DR EvolutionaryTrace; Q5MWV9; -.
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; 2.150.10.10; -; 2.
DR InterPro; IPR008640; Adhesin_Head_dom.
DR InterPro; IPR008635; Coiled_stalk_dom.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF03895; YadA_anchor; 1.
DR Pfam; PF05658; YadA_head; 1.
DR Pfam; PF05662; YadA_stalk; 20.
DR SUPFAM; SSF101967; SSF101967; 2.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane; Membrane;
KW Protein transport; Signal; Transmembrane; Transmembrane beta strand;
KW Transport; Virulence.
FT SIGNAL 1..47
FT /evidence="ECO:0000305|PubMed:15534369"
FT CHAIN 48..3082
FT /note="Autotransporter adhesin BadA"
FT /id="PRO_0000448367"
FT TRANSMEM 3028..3039
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:15534369"
FT TRANSMEM 3044..3051
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:15534369"
FT TRANSMEM 3055..3065
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:15534369"
FT TRANSMEM 3070..3082
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:15534369"
FT REGION 48..2901
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 48..376
FT /note="Binds to host cells"
FT /evidence="ECO:0000269|PubMed:18627378"
FT REGION 53..2850
FT /note="Does not bind host cells, no host proangiogenic
FT cytokine induction, collagen or fibronectin, no
FT autoagglutination"
FT /evidence="ECO:0000269|PubMed:21981119"
FT REGION 470..2850
FT /note="Required to bind fibronectin, not required for
FT surface expression on bacteria, bacterial
FT autoagglutination, host cell binding, collagen binding or
FT host proangiogenic cytokine induction"
FT /evidence="ECO:0000269|PubMed:18627378"
FT REGION 2902..3027
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 3028..3082
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0,
FT ECO:0000305|PubMed:15534369"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:3D9X"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:3D9X"
FT HELIX 485..495
FT /evidence="ECO:0007829|PDB:3D9X"
SQ SEQUENCE 3082 AA; 327543 MW; 3933F42E176C038E CRC64;
MKKLSVTSKR QYNLYASPIS RRLSLLMKLS LETVTVMFLL GASPVLASNL ALTGAKNLSQ
NSPGVNYSKG SHGSIVLSGD DDFCGADYVL GRGGNSTVRN GIPISVEEEY ERFVKQKLMN
NATSPYSQSS EQQVWTGDGL TSKGSGYMGG KSTDGDKNIL PEAYGIYSFA TGCGSSAQGN
YSVAFGANAT ALTGGSQAFG VAALASGRVS VAIGVGSEAT GEAGVSLGGL SKAAGARSVA
IGTRAKAQGE ESIAIGSSVK NGDKDGSAVA QGAKAIAIGS NSISFQHYAV AVGAKAHALL
SKTVALGYDS VADVDAGIRG YDPVEDEPSK DVSFVWKSSL GAVSVGNRKE GLTRQIIGVA
AGTEDTDAVN VAQLKALRGM ISEKGGWNLT VNNDNNTVVS SGGALDLSSG SKNLKIVKDG
KKNNVTFDVA RDLTLKSIKL DGVTLNETGL FIANGPQITA SGINAGSQKI TGVAEGTDAN
DAVNFGQLKK IETEVKEQVA ASGFVKQDSD TKYLTIGKDT DGDTINIANN KSDKRTLTGI
KEGDISKDSS EAITGSQLFT TNQNVKTVSD NLQTAATNIA KTFGGGAKYE DGEWIAPAFK
VKTVTGEGKE EEKRYQNVAD ALAGVGSSIT NVQNKVTEQV NNAITKVEGD ALLWSDEANA
FVARHEKSKL GKGASKATQE NSKITYLLDG DVSKDSTDAI TGKQLYSLGD KIASYLGGNA
KYEDGEWTAP TFKVKTVKED GKEEEKTYQN VAEALTGVGT SFTNVKNEIT KQINHLQSDD
SAVVHYDKNK DETGGINYAS VTLGKGKDSA AVTLHNVADG SISKDSRDAI NGSQIYSLNE
QLATYFGGGA KYENGQWTAP IFKVKTVKED GEEEEKTYQN VAEALTGVGT SFTNIKSEIT
KQIANEISSV TGDSLVKKDL ATNLITIGKE VAGTEINIAS VSKADRTLSG VKEAVKDNEA
VNKGQLDKGL KHLSDSLQSD DSAVVHYDKK TDETGGINYT SVTLGGKDKT PVALHNVADG
SISKDSHDAI NGGQIHTIGE DVAKFLGGAA SFNNGAFTGP TYKLSNIDAK GDVQQSEFKD
IGSAFAGLDT NIKNVNNNVT NKFNELTQNI TNVTQQVKGD ALLWSDEANA FVARHEKSKL
GKGASKATQE NSKITYLLDG DVSKDSTDAI TGKQLYSLGD KIASYLGGNA KYENGEWTAP
TFKVKTVKED GKEEEKTYQN VAEALTGVGA SFTNVKNEIT KQINHLQSDD SAVVHYDKNK
DETGGINYAS VTLGKGKDSA AVTLHNVADG SISKDSRDAI NGSQIYSLNE QLATYFGGGA
KYENGQWTAP IFKVKTVKED GEEEEKTYQN VAEALTGVGT SFTNIKSEIT KQIANEISSV
TGDSLVKKDL ATNLITIGKE VAGTEINIAS VSKADRTLSG VKEAVKDNEA VNKGQLDTNI
KKVEDKLTEA VGKVTQQVKG DALLWSNEDN AFVADHGKDS AKTKSKITHL LDGNIASGST
DAVTGGQLYS LNEQLATYFG GGAKYENGQW TAPTFKVKTV NGEGKEEEQT YQNVAEALTG
VGASFMNVQN KITNEITNQV NNAITKVEGD SLVKQDNLGI ITLGKERGGL KVDFANRDGL
DRTLSGVKEA VNDNEAVNKG QLDADISKVN NNVTNKFNEL TQNITNVTQQ VKGDALLWSD
EANAFVARHE KSKLEKGVSK ATQENSKITY LLDGDISKGS TDAVTGGQLY SLNEQLATYF
GGGAKYENGQ WTAPTFKVKT VNGEGKEEEQ TYQNVAAAFE GVGTSFTNIK SEITKQINNE
IINVKGDSLV KRDLATNLIT IGKEIEGSVI NIANKSGEAR TISGVKEAVK DNEAVNKGQL
DTNIKKVEDK LTEAVGKVTQ QVKGDALLWS NEDNAFVADH GKDSAKTKSK ITHLLDGNIA
SGSTDAVTGG QLYSLNEQLA TYFGGGAKYE NGQWTAPTFK VKTVNGEGKE EEKTYQNVAA
AFEGVGTSFT NIKSEITKQI ANEISNVTGD SLVKKDLDTN LITIGKEIAG TEINIASVSK
ADRTLSGVKE AVNDNEAVNK GQLDANISKV NNNVTNKFNE LTQSITNVTQ QVKGDALLWS
DEANAFVARH EKSKLEKGVS KATQENSKIT YLLDGDISKG STDAVTGGQL YSLNEQLATY
FGGGAKYENG QWTAPTFKVK TVNGEGKEEE QTYQNVAAAF EGVGTSFTNI KSEITKQINN
EIINVKGDSL VKRDLATNLI TIGKEIEGSV INIANKSGEA RTISGVKEAV KDNEAVNKGQ
LDTNIKKVED KLTEAVGKVT QQVKGDALLW SNEDNAFVAD HGKDSAKTKS KITHLLDGNI
ASGSTDAVTG GQLYSLNEQL ATYFGGGAKY ENGQWTAPTF KVKTVNGEGK EEEKTYQNVA
AAFEGVGTSF THVKNEITKQ INHLQSDDSA VVHYDKDDKN GSINYASVTL GKGKDSAAVA
LHNVADGSIS KDSHDAINGG QIHTIGEDVA KFLGGDAAFK DGAFTGPTYK LSNIDAKGDV
QQSEFKDIGS AFAGLDTNIK NVNNNVTNKL SELTQNITTV TQQVKGNALL WSDEANAFVA
RHEKSKLEKG ASKAIQENSK ITYLLDGDVS KGSTDAVTGG QLYSMSNMLA TYLGGNAKYE
NGEWTAPTFK VKTVNGEGKE EEQTYQNVAE ALTGVGTSFT NIKSEIAKQI NHLQSDDSAV
IHYDKNKDET GTINYASVTL GKGEDSAAVA LHNVAAGNIA KDSRDAINGS QLYSLNEQLL
TYFGGDAGYK DGQWIAPKFH VLQFKSDGSS GEKESYDNVA AAFEGVNKSL AGMNERINNV
TAGQNVSSSS LNWNETEGGY DARHNGVDSK LTHVENGDVS EKSKEAVNGS QLWNTNEKVE
AVEKDVKNIE KKVQDIATVA DSAVKYEKDS TGKKTNVIKL VGGSESEPVL IDNVADGKIE
ADSKQAVNGG QLRDYTEKQM KIVLDDAKKY TDERFNDVVN NGINEAKAYT DVKFEALSYT
VEEVRKEARQ AAAIGLAVSN LRYYDIPGSL SLSFGTGIWR SQSAFAIGAG YTSEDGNIRS
NLSITSSGGQ WGVGAGITLR LK
