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Database: UniProt
Entry: A0A4V3DZ21_9HYPH
LinkDB: A0A4V3DZ21_9HYPH
Original site: A0A4V3DZ21_9HYPH 
ID   A0A4V3DZ21_9HYPH        Unreviewed;       886 AA.
AC   A0A4V3DZ21;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   02-APR-2025, entry version 17.
DE   SubName: Full=Ca2+-binding RTX toxin-like protein {ECO:0000313|EMBL:TDR94849.1};
GN   ORFNames=EV668_2139 {ECO:0000313|EMBL:TDR94849.1};
OS   Enterovirga rhinocerotis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylobacteriaceae; Enterovirga.
OX   NCBI_TaxID=1339210 {ECO:0000313|EMBL:TDR94849.1, ECO:0000313|Proteomes:UP000295122};
RN   [1] {ECO:0000313|EMBL:TDR94849.1, ECO:0000313|Proteomes:UP000295122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25903 {ECO:0000313|EMBL:TDR94849.1,
RC   ECO:0000313|Proteomes:UP000295122};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:TDR94849.1}.
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DR   EMBL; SNZR01000011; TDR94849.1; -; Genomic_DNA.
DR   RefSeq; WP_133769707.1; NZ_SNZR01000011.1.
DR   AlphaFoldDB; A0A4V3DZ21; -.
DR   OrthoDB; 7975253at2; -.
DR   Proteomes; UP000295122; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd04277; ZnMc_serralysin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR013858; Peptidase_M10B_C.
DR   InterPro; IPR050557; RTX_toxin/Mannuronan_C5-epim.
DR   InterPro; IPR003995; RTX_toxin_determinant-A.
DR   InterPro; IPR034033; Serralysin-like.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR   PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR   Pfam; PF00353; HemolysinCabind; 5.
DR   Pfam; PF08548; Peptidase_M10_C; 1.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   PRINTS; PR01488; RTXTOXINA.
DR   SUPFAM; SSF51120; beta-Roll; 4.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295122};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          765..817
FT                   /note="Peptidase M10 serralysin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08548"
FT   REGION          641..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..657
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  90952 MW;  64D2FB6F510A2389 CRC64;
     MATLSITPQQ IDNGLLYPNF YWPAGTITYS VPDGDTLWAS NYGSSEPTTG YSEFNAAQAA
     QFVAAIELWD SYIANSMVRV DDGATYGDIR GAFTDIADPQ VGGQANAPPF QGNRSSAREG
     DVWIDTTRTG SGFATGTQDF QLLLHEIGHA LGLKHPFETP TLPAEYDNHA YTVMSYTPAD
     HRIIFSGGGG SIFWSQAPTA DKTPMVLDIA AIQSRYGADT QTGAGSTTYA FTDADLEARQ
     AIYDASGNDT IDLSALSRGS TLDLRPGSYS DLAYYAKADQ IADTKARFPG FESFIENGFN
     QPGVAVYEWT RNVGIAFSTV IENAMGSAFA DTIIGNSAAN RIGGGLGRDV LTGGGGSDNF
     HGTAAALAGD RITDLSNGET ITLDGSTASI TAVSLASGTL TVSYRASAGG SVQSFAMTVS
     GGVSGVSFSG RTITFGEADR NDTFVGQAGN QTYDGGAGID TVNYAAASGA LTVDLALTGF
     QSVGGGFGSD RLLSIENLRG GTGSDRLSGS ASANTIWGGA GNDTILGRNG ADILWGEAGN
     DILDGGAGAD RMFGGAGNDT YIVDAASDSV REDRIAGTDD GGIDLVKASV THTLRAFVEN
     LTLTGSGAIF GTGNALANTI IGNDAANRLY GKDGNDRLDG RAGNDLLRGG NGNDTLTGGA
     GADDMDGENG SDTYYVDASD TVRDRGASGI DTVIASSTFS LKGGDGIENL RLATNATSGN
     LTGNELGNAI TAYGGNNVLL GLAGNDTIRA GAGNDTLRGG LGADRLYGEA GADTFVFAKG
     ESLAVAGATD IIHDFTTRVD HIDLAIVSGS AAAAFYTEVK VASDSFTALK NAAEAAMSGS
     QRIVFVAGTT DGWLFWSTNG SDGTVEEAVR LTGRNSLAGF DRADLI
//
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