ID A0A1C6P9W7_9BURK Unreviewed; 721 AA.
AC A0A1C6P9W7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Head domain of trimeric autotransporter adhesin {ECO:0000313|EMBL:SCK39947.1};
GN ORFNames=VAR608DRAFT_3767 {ECO:0000313|EMBL:SCK39947.1};
OS Variovorax sp. HW608.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1034889 {ECO:0000313|EMBL:SCK39947.1, ECO:0000313|Proteomes:UP000198203};
RN [1] {ECO:0000313|Proteomes:UP000198203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HW608 {ECO:0000313|Proteomes:UP000198203};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000256|ARBA:ARBA00005848}.
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DR EMBL; LT607803; SCK39947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6P9W7; -.
DR Proteomes; UP000198203; Chromosome i.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd12820; LbR_YadA-like; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.40.4050; -; 1.
DR Gene3D; 6.10.250.2040; -; 6.
DR Gene3D; 3.30.1300.30; GSPII I/J protein-like; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
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; 3.
DR Pfam; PF05662; YadA_stalk; 8.
DR SUPFAM; SSF101967; Adhesin YadA, collagen-binding domain; 7.
DR SUPFAM; SSF54523; Pili subunits; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Membrane {ECO:0000256|ARBA:ARBA00022452};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 12..51
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 70..92
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 132..164
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 194..216
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 256..279
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 316..334
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 373..413
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 442..462
FT /note="Trimeric autotransporter adhesin YadA-like head"
FT /evidence="ECO:0000259|Pfam:PF05658"
FT DOMAIN 451..477
FT /note="Trimeric autotransporter adhesin YadA-like head"
FT /evidence="ECO:0000259|Pfam:PF05658"
FT DOMAIN 479..505
FT /note="Trimeric autotransporter adhesin YadA-like head"
FT /evidence="ECO:0000259|Pfam:PF05658"
FT DOMAIN 570..602
FT /note="Trimeric autotransporter adhesin YadA-like stalk"
FT /evidence="ECO:0000259|Pfam:PF05662"
FT DOMAIN 663..721
FT /note="Trimeric autotransporter adhesin YadA-like C-
FT terminal membrane anchor"
FT /evidence="ECO:0000259|Pfam:PF03895"
SQ SEQUENCE 721 AA; 69787 MW; E1C51F2DC22932A8 CRC64;
MTVDGIDAGG QKIVNVADGT DASDAATVGQ VNAAASAAMA DAVKYDDASH NSVTLGGTAY
DSATGTGGTK VSNVAKGTAD SDAVNVAQLK DSGLIDSNGN TLNAVTYDDA TKGSITLGGT
PYDSVTGTGG TKIGNVAKGT VDSDAVNVAQ LKDSGLIDNN GNTLNAVTYD DATKGSVTLG
GTPYDSATGT GGTKIGNVAK GTADSDAVNV SQLKDSGLID GNGNTLNAVT YDDATKGSVT
LGGTPYDSAT GTGGTKISNV AKGTGDSDAV NVSQLKDAGL IDSNGNTLNA VTYDDATKRS
VTLGGVGATT PVRLGNVADG TDDHDAVNVS QLRNSGLLDG NGNTLNAVTY DDATKGIVTL
GGVGATTPVR LGNVADGNIA AGSRDAVNGG QIATLVSQIN GLDNRVTNIE ANGTGGGSSL
PYVDGNANGS SSNNADAGST AGVAVGYNAK ATGENASVLG QNATALGSYG TAIGNDSYAA
GPNDTALGGN AKVHADGSVA VGANATVTSA AATNAVAVGA DTQVSAASGT AIGQGASVAA
AATGGVALGQ GSVADRANTV SVGTATNQRQ ITNVAAGSQA TDAVNVDQLT SVVNGLGGGA
SIDSTTGAVT GPSYQLSDGT YSNVGDALSS LDNRVNAANQ AIGDLSRNAY SGIAAATALT
MIPDVDKDKK LSLGIGAGSY KGYHAFAIGG TARITQNIKM RAGLGRSGSG TTAGVGASYQ
W
//
