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Database: UniProt
Entry: A0A0M2V2F4_9BACT
LinkDB: A0A0M2V2F4_9BACT
Original site: A0A0M2V2F4_9BACT 
ID   A0A0M2V2F4_9BACT        Unreviewed;       333 AA.
AC   A0A0M2V2F4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Bacterial Ig-like domain (Group 1) {ECO:0000313|EMBL:KKO20884.1};
DE   Flags: Fragment;
GN   ORFNames=BROFUL_00387 {ECO:0000313|EMBL:KKO20884.1};
OS   Candidatus Brocadia fulgida.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO20884.1, ECO:0000313|Proteomes:UP000034954};
RN   [1] {ECO:0000313|EMBL:KKO20884.1, ECO:0000313|Proteomes:UP000034954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KKO20884.1};
RX   PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA   Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA   Keltjens J.T., Jetten M.S.;
RT   "Identification of the type II cytochrome c maturation pathway in anammox
RT   bacteria by comparative genomics.";
RL   BMC Microbiol. 13:265-265(2013).
CC   -!- SIMILARITY: Belongs to the intimin/invasin family.
CC       {ECO:0000256|ARBA:ARBA00010116}.
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:KKO20884.1}.
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DR   EMBL; LAQJ01000050; KKO20884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2V2F4; -.
DR   Proteomes; UP000034954; Unassembled WGS sequence.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR003344; Big_1_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR48148; KERATINOCYTE PROLINE-RICH PROTEIN; 1.
DR   PANTHER; PTHR48148:SF2; KERATINOCYTE PROLINE-RICH PROTEIN; 1.
DR   Pfam; PF13229; Beta_helix; 1.
DR   Pfam; PF02369; Big_1; 1.
DR   SMART; SM00634; BID_1; 1.
DR   SMART; SM00710; PbH1; 3.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS51127; BIG1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000034954}.
FT   DOMAIN          171..264
FT                   /note="Big-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51127"
FT   REGION          255..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..319
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKO20884.1"
FT   NON_TER         333
FT                   /evidence="ECO:0000313|EMBL:KKO20884.1"
SQ   SEQUENCE   333 AA;  34603 MW;  FF7CB52426B8AC34 CRC64;
     DGTSGNPITF TSNGATPAPG DWEGIVFYNS TDDASTILDY CTVEYGGYDT YNSNINCNQA
     SPTIQRCLIR NSDGYGIHTT GSGAQPLISC STITDNTHGV YVASGNPTIE NCSIAGNTSY
     GVFTNTFIYA ENNWWGNASG PSGVGPGSGD AVSSDVDYTP WLSAYNSCLE TIVLSPSSET
     NLIGTQHTVT ATVTDDASDP MEGIVLFFYI TSGPHAGLNS NVTTDSNGQA TFTYTGTLEG
     TDIIEASFTD FHGRTITSGP VTKTWESLPP TPTPTPSPTP TPEPTPSPTP SPTPEPTPSP
     TPSPTPSPTP SPTPTPAACP CPDAEACYSF DEG
//
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