ID A0A0Q7DYT6_9CAUL Unreviewed; 1756 AA.
AC A0A0Q7DYT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SbsA Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASC65_10380 {ECO:0000313|EMBL:KQW82611.1};
OS Brevundimonas sp. Root1279.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW82611.1, ECO:0000313|Proteomes:UP000050923};
RN [1] {ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW82611.1, ECO:0000313|Proteomes:UP000050923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1279 {ECO:0000313|EMBL:KQW82611.1,
RC ECO:0000313|Proteomes:UP000050923};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQW82611.1}.
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DR EMBL; LMEB01000006; KQW82611.1; -; Genomic_DNA.
DR RefSeq; WP_056452430.1; NZ_LMEB01000006.1.
DR STRING; 1736443.ASC65_10380; -.
DR OrthoDB; 7202227at2; -.
DR Proteomes; UP000050923; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2700; -; 3.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 5.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR040853; RapA2_cadherin-like.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR032812; SbsA_Ig.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR46580:SF3; ATP_GTP-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46580; SENSOR KINASE-RELATED; 1.
DR Pfam; PF13205; Big_5; 1.
DR Pfam; PF17803; Cadherin_4; 1.
DR Pfam; PF13517; FG-GAP_3; 2.
DR Pfam; PF00353; HemolysinCabind; 6.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; beta-Roll; 4.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000050923};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 326..434
FT /note="SbsA Ig-like"
FT /evidence="ECO:0000259|Pfam:PF13205"
FT DOMAIN 1036..1113
FT /note="RapA2 cadherin-like"
FT /evidence="ECO:0000259|Pfam:PF17803"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 175806 MW; EE1298A1A0AD61B9 CRC64;
MPVTFSEQST ATFPQPAAGG RMSFIDADSD GDLDILYQTG ANGTAFQYAR SNGDGTYTIL
ALGSSPFAGL TIPDHNGGNF HVGDIDGDGD MDLWAGQSTG AGTGSYFRND NGTFTSQSSA
TYPQPGASSR VVMADFDGDG DADMLYQTVG NGTAFQYAQS NGDGTYTLLA QAASPFAGVT
LLDNSGGTHV AADFDGDGDL DLWNTQASTT GAYFRNDGGT FSSQSSATFP APAAITRIVV
GDFDSDGDAD ILYQTAGDGS AWQYARSNGD GTMTILSQAS SPFAGVTLVN HNGSNFIAGD
VDGDGDHDVL GVLNSTQGEF YLANGKPPEI VSSTPSDNGT GVAVGANIVL TFDESVVKGS
GNIYIYRGDG TLIETISVGS AQVTGSGTTW TIDPSVTLAG LTNYYVLTDD GIFADADGSI
FAGISDAITL NFTTAAANTA PTFTNLNGDT AGFTENVSGA VRLDMGQNAT VADAEQANFN
GGALTVTITA NGVAAQDVLS VANIGTGAGQ ISVSGANISY QGVQIATFTG GTAGAALTIT
LDADATPAAT QALVRALQYN NTSDAPTSAT RTITTVLTDG AGGTSATQTT TVTLSAANDP
HTGGASITGT ATENQVLTAV STIADPDGLG TLHYQWQRDT GGGFVNVGSD QATYTLGDAD
VGGVIRTVIY YTDAGGTVES ATSASTAAIA ATNDPHTGGA ALTGTATENQ VLTAVSTLAD
ADGLGTLHYD WQRDTGAGFV SIGAADQATY TLGDADVGGV VRVVISYTDG QGFAESATSA
GTAAIAGVND PHTGGASITG TATEDQVLTA VSTIADADGL GTLHYQWQRD TGAGYVNVGS
DQATYTLGDA DVGGVVRVVI YYTDAGGTVE SATSAGTAAI ANVNDAPTLS LTAATATFTE
GDAAVDLFSG LSAANIESGQ ELSVRLSITG VVDGANESIV LSGVPMLLIP GSPDIQPAPG
GAVMYQITAG ALPGELILTI VGMTSTSHLE QVLNGMSYQV TGDNPTAGDR QITVVSITDN
GGTANGGVNT SAVNETATIT VVAADDAPVA GDDSDSTLES VVLNGSVFGN DSDVDGPALE
ISEVNGSAAA VGSQISLASG ALLTVNADGT YSYDPNDAFN ALSGPASGGT NLTATDTFTY
TLTNGNTATV TVTIVGEDSP GDSVQGDSGD NTLTAGDGED TLVGGGGNDA LDGGDGEDTA
DYSGSTGGVH IRLNGGFGSD GEGGTDTLTN IENLIGSANN DILIGAAGGN LLSGGAGSDV
LIGLDGDDLL VGGAGAANQL QGGQGDDTYF VEANDTVVEL ENQGHDRIFT SRNNMTLVAN
VEELHFTGAG PFTGIGNDLD NTIVGGVFDD TLVGGFGNDI LNGGTGGSDT VSYAATGLAV
FVNLANNIAA GFLGTDTLIS IENVIGSSSN DVIAGDANAN RLSGGAGDDF LTGRGGNDVL
QGGLGVDTVD YQDAASGVVV RLDLSTAQDG DGGVDTLSSI ERIWGSAFND LIIGNAGANS
LSGGEGADVL IGRDGNDTLI GGSGAANTLY GGAGDDFYVV SANDTIHELA GEGTDTVQTD
RAYYALAANI ENLEYDDDGD FAGVGNALNN VITGGVGRDT LRGGQGNDTL NGGDGYDTAQ
YAGTLSQYTI ESLGGGQYRV TDTVAGRDGV DIVDGIEQLR FSDQISVLGG AGAPVLSAKE
MAAAVSPLMD DGFFLPKDLD LPQILPDAFD PFAAPAFDGP VFALASEATA GLADSGMLHA
ALNVHHEAVF DDDWLM
//
