BMAC_BRUSU
ID BMAC_BRUSU Reviewed; 3420 AA.
AC A0A0H3GGE2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Adhesin BmaC autotransporter {ECO:0000305};
DE AltName: Full=Brucella monomeric autotransporter {ECO:0000303|PubMed:22321605};
DE Flags: Precursor;
GN Name=bmaC {ECO:0000303|PubMed:22321605};
GN OrderedLocusNames=BRA1148 {ECO:0000312|EMBL:AAN34307.1},
GN BS1330_II1139 {ECO:0000312|EMBL:AEM20583.1};
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP FUNCTION, FIBRONECTIN-BINDING, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=1330;
RX PubMed=22321605; DOI=10.1111/j.1462-5822.2012.01771.x;
RA Posadas D.M., Ruiz-Ranwez V., Bonomi H.R., Martin F.A., Zorreguieta A.;
RT "BmaC, a novel autotransporter of Brucella suis, is involved in bacterial
RT adhesion to host cells.";
RL Cell. Microbiol. 14:965-982(2012).
CC -!- FUNCTION: Fibronectin-binding protein, which is involved in adhesion to
CC host cells and in the infective process. Mediates the binding of B.suis
CC to the extracellular matrix and to non-phagocytic cells via cell-
CC associated fibronectin. {ECO:0000269|PubMed:22321605}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:22321605}. Cell
CC outer membrane {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Localizes at one cell pole (PubMed:22321605). The
CC C-terminal autotransporter region is probably inserted into the outer
CC membrane (Probable). {ECO:0000269|PubMed:22321605, ECO:0000305}.
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:Q45340}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is impaired in the adhesion of
CC B.suis to immobilized fibronectin and host cells.
CC {ECO:0000269|PubMed:22321605}.
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DR EMBL; AE014292; AAN34307.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20583.1; -; Genomic_DNA.
DR RefSeq; WP_006191504.1; NZ_KN046805.1.
DR SMR; A0A0H3GGE2; -.
DR EnsemblBacteria; AEM20583; AEM20583; BS1330_II1139.
DR GeneID; 45054131; -.
DR KEGG; bms:BRA1148; -.
DR KEGG; bsi:BS1330_II1139; -.
DR PATRIC; fig|204722.22.peg.2740; -.
DR HOGENOM; CLU_000353_0_0_5; -.
DR OMA; NVADANL; -.
DR Proteomes; UP000007104; Chromosome II.
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 CDD; cd01344; PL2_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 2.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR043990; AC_1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR013425; Autotrns_rpt.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF18883; AC_1; 1.
DR Pfam; PF12951; PATR; 18.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 8.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR TIGRFAMs; TIGR02601; autotrns_rpt; 17.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Membrane; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..72
FT /evidence="ECO:0000305|PubMed:22321605"
FT CHAIN 73..3420
FT /note="Adhesin BmaC autotransporter"
FT /id="PRO_0000438295"
FT DOMAIN 3138..3420
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
SQ SEQUENCE 3420 AA; 337794 MW; 9D60CDD3FB5372D6 CRC64;
MPNLANQDFT QFKREQQTAP AWFRILRGGR MTKWKGKVAS YAPHVAPAIG WAFSRTLQLS
LISLVMAGTA AASDRYWDSN GTAVGRGGSG AWNTSNAFWS PSGDGVSGPY SAWNNAAFDT
AIFGGTAGTV TLGSPITVGA MTFETTGYIL SGNTLTLGTA TPTITTSSGT TTINSVLAGT
NGLTKAGDGI LSLTGANTFS GNIIVTGGTL SVNSSAALGA AANEISLANG AGLNSSGSLA
GRSVTLTGGQ AAIGGAGVGD AHFTGAGGLR ASSSVTLSDD SNDYTGQTSL SSGGTLFFSS
IGNLGEVSAL GAPVDEAAGT ISLVVGSSAS ASATYTGSGA SSNRNWQLSS RFYANSTISN
RGSGTLTLTG NIFNNHTNSS LSARNINFDA GTADIELLGT ISSNNNGVGV VFGGTAGRTI
KVSGDNTFGG AAIIQNITVQ VGSLKNTGDP SALGTGTGAA GAISINSGIL SYLGAGDSSD
RNFTAQNNAI LANDGTGALT LSGDVALTGT LTLGGSFAGT NTLAGTVSGT GNLRVDGAGS
WILSSANTFT GDVGVNSGTL VVGNMQALGT TPKAATVNGG TLDLGAFDTT LSSLSGTGGN
VNLGGATLTV KGSTSTDFAG SMTGSGNLLK QGTSTLTLTG ASSFTGDTTI NGGAISLNFK
NATALTDNIL STSSTLNLAG GTFNVIGMDN AANSQTVDGL NVTTGNNKIT TTSGSGGTLT
LNLGAINRTG GFIDFGINAD TTITTTSATL GGWATVNSTD YAKVDGGVIK ALDESDYANK
DDAGTWANGD IVSDAGGAAN TPYFGTVGTG LQLGGLKYTA AANSTVTIAA GQTLGVNGTI
IVANTVGNTN QTINGGSLTG ITGGGVLGVL QTGTGTFTIQ STITDNGGAI GFTKAGAGSV
TLTGQNTYSG VTTLSGGILT VTQMANAGMA SGIGQSTADP ANLMLESGTF RYTGGSVTTD
RGFTLVNGGP ARVIEVTGSG SNLAFSGLVT SPDDAGFEKK GAGTLTFLNG SNDYIGATTV
SGGTLAVSTL ADGGQVSSLG KSGSDATNLI LAGGALNYLG STTSSDRSFT LGAGNGSIGV
ANAGTTLSMS GTAVGTGGLT KLGDGTLILS GTNTYTGNTA VNAGVLRAGS AQAFGPSGLM
TVGNGASLEL GGYDITVSGL LGAGTVDLGG NTLTSSGSAA NSFTGKITGT GGFTRTGGST
QTLSGCNSDY TGKTTIASNG TLSVDCLKNG GQASSIGASS NAPDNLVLNN GTLSYTGNTV
TTDRGFTIQG GTGAISVTDA ATTLTFSGQV VGTGALQKRG TGTLVLMNSN SYRGGTSVDA
GTLRAGSSGA FGGGSMSLSN AAGAILDLDG FDTSVTSLSG GGALGGNVAL GGATLTISSG
NSNGTSYTGA ITGIGNFVKN GNGTQRLTGC ASSYSGSTTI NGGVLEDSCL ADGGSVSSIG
MSSADADNLV INGGVLRYTG SGDSTDRQFT LGASGGNSIE SEGTGAILFT SNAAVTFAAA
NTAQTLTLAG TNTDDNELGA QLTNNGSGIT SLTKTDTGTW FLTNSDSTYT GVTKINGGVL
SVDKLANGGL ASSIGASSSA ASNLIIGNDS TLRYLGTGDT TDRLFTLASG LTYIESSGSG
AIVFTDTGQV ALADNNQART IALGGKNTGD NTLAGSIGDA GTGKTTLAKN DDGTWVLTGN
NTFTGPTNIN KGLLKIGNGG TTGSLTSDIV VTDGGLIFNR SDTLNYGGLI SGAGFVTQSG
SGTTILTGAN SYTGATSVSA GTLLVNGDQS AATGQTSVAN GSILGGSGII GGNVVVTDGA
LAPGSNGAGT LTINGSLALS AGSILSMQLG QAGVAGGALN DLIEVKGNLT LDGTLDVAET
AGGSYGPGIY RLINYTGSLT DNGLDIGMLP NGAGAIQTAV AGQVNLLAGG TNFNFWDGDV
GPKFNSAVDG GNGTWQNSSG NNNWTDATGN INASYSDGAF AIFTGTAGTV TIDNSLGQVK
AEGMQFAIDS YAVTGDKLEL TGPQSTIRVG DGTTAGAAYI ATINSVLTGN TQLEKTDAGT
LVLTGANSYT GGTAINGGTI RISSDDNLGV ASSDISFDGG ALNTTANIAT DRAIILTGAG
TLLTDASTTL SLSGPISGTG ALTKSGTGTL LLSGTAVHTG GTTITAGTLQ IGNGGTDGSI
DGNIVNNGAL VFDRAGTLAY TGSISGTGTL TKNGSSTLTM TGTSTYTGET TVSAGTLALQ
AGGQIKGTAS LTVDGGAEVL IDGSGSQFAT GAGASVVGTG TVTVRDGGTA SFDSLTTSNA
TGTNSTITVA GSGSQMTQTG IATFGLAGTA TVDILDGGTM ISSGASVFVG GQLPMDATGQ
VTISGAGSQW TIANALYARR GSITVDDGGV VTAGSAVIGY ADTGINNPET DLVVTGAGSR
FETTGELAIT NSAANAARGS ITIADGGVVK VGGGALAMGP GNAVLNIGAA AGGSPAHAGT
LDAGTVTMAV GSNQINFNHD DASTTFSATI SGAGSVSQNG PGATLLTGNN SYAGLTTVTA
GSLYIDGDQS MATGLTTVNP GGTLGGTGTI GGDVTVASGG AINPGSFGMA PGTLNINGDL
TLASGSTQSF SFGQANIPGG PLNDLINVGG DLVLAGTLQV DTSAGGTMDP GIYRVFNYTG
TLSQNAWTVN LPSPDFYVQT SVAQQINLVN TAGLALRFWD GADPQNKNNG KIEGGNGIWQ
AFGSAPDNGN DNWTETGNIN APFQDATFAV FTGEKGTVTV DDSKGAINVS GIQFVTDGYI
VNGDAINLVG ASGSTIRVGD GTTGGTDTVA SIDAEITGAS QLIKADMGTL ILTGDNSYTG
GTKITGGTLQ VAKDSALGAR TGELILDGGT LNTTADMTID RSVTVDQAGT LDIDTGTTLK
IDGVLSGAGA FVKTGAGRLE LAGDDHTYNG DASIASGTLA LTGALGGTMN VGIDGRLEAT
GRVGATTNSG VIALDQEGFG SLTVNGNYTG KDGRLEIATV LGDDTSLTNR LVIDGDMAGT
TQVSVTNRGG LGAQTVEGIK IIQVGGASNG MFLLAGDYMF NGEQAVVAGA YGYRLYKGGV
STPADGNWYL RSALLNPETP TNPTDPETPL YQPGVPLYES YAGSLQQLNK LGTLQQRVGN
RVWAKHPVPA QSDENGAGPS GNNGIWARIE AAHAEFDPKQ STSRASYDAD IWKFQTGIDG
MFAETASGKF IGGVYVQYET VSSSVSSPFG NGSIESSGYG AGATLTWYGE SDFYIDGVAQ
INWFDSDLNS ATLGRQLVDG NRAVGYSLSV ETGQKIEIGE GWSLTPQAQL AYSAIRFDDF
KDAFDTSVSP ENDHDLTGRL GLAINRDAEW LDAQGRRVAM HIYGIGNLYY GFAGASKVDV
SSVRFVSGNE RLRGGIGLGG TYDWADSKYS LYGETRFDTS LQNFGDSNVI AGSVGLRVRW
