ID A0A2N4YFU9_9RHOB Unreviewed; 2958 AA.
AC A0A2N4YFU9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PLL12144.1};
GN ORFNames=C0V75_14805 {ECO:0000313|EMBL:PLL12144.1};
OS Tabrizicola sp. TH137.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL12144.1, ECO:0000313|Proteomes:UP000234539};
RN [1] {ECO:0000313|EMBL:PLL12144.1, ECO:0000313|Proteomes:UP000234539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH137 {ECO:0000313|EMBL:PLL12144.1,
RC ECO:0000313|Proteomes:UP000234539};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: 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:PLL12144.1}.
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DR EMBL; PKRQ01000004; PLL12144.1; -; Genomic_DNA.
DR OrthoDB; 6305173at2; -.
DR Proteomes; UP000234539; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 19.
DR InterPro; IPR006946; DGR2-like_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR028992; Hedgehog/Intein_dom.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF04862; DUF642; 2.
DR Pfam; PF00353; HemolysinCabind; 32.
DR Pfam; PF13403; Hint_2; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; beta-Roll; 14.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 31.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000234539};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 301..450
FT /note="DUF642"
FT /evidence="ECO:0000259|Pfam:PF04862"
FT DOMAIN 516..664
FT /note="DUF642"
FT /evidence="ECO:0000259|Pfam:PF04862"
FT DOMAIN 2761..2898
FT /note="Hedgehog/Intein (Hint)"
FT /evidence="ECO:0000259|Pfam:PF13403"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1970..2111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2158..2186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2279..2479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2586..2605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2610..2639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2452..2467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2619..2633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2958 AA; 291512 MW; 5F183EA9555B8B0E CRC64;
MSFQINNVAI QPVAALITLN FSSATTQTIN LTLNLGQLLT QSGTLTADDP NNNDLITRGE
TVDHNNPDGI LGLLDAVPDL NNATVLGVGQ MSALITGAFV TYPVILVESG GSQYLLYPDG
GPDLLSIVTG TINTNITFFR DGAIDGNGNV VIPPDANPDG VVNGTSAGQV MNPGFTDAQG
DQIDGDDGND DVIDAAGGND TVNAGLGNDT VAAGAGNDIV EGAAGADAIG GGDGDDSLSG
GSGRDTLTGD EGRDTVSGGA GNDVLEGSGG NDSLIGGAGA DSVFGGSGND VLLGDGDDQQ
NLLVNGSFEI GRTSNNTNNL NAQLTGWSSN TPNNLIESWG QGFAGTSASD GSGSIELDRD
GARVDSVFQD ITTEPGTTYT ISVDARSRPS TSDSFQIVID GNVVGTYSPG QSFATYSLNY
TATNSTTRIE FRELANQNNG EGVVLDNVHV IEAVPDFDDT LDGGEGDDTI DGGAGNDSLL
GGSGNDSLIG SIGDDTLFGG SGDDVLLGEG SGSQNLVQNA SFETNRTADG FNNLNATLPG
WSSNTSGNLI ESWGQGFLGT SASDGRGYVE IDRDPARVDS IWQDIGTEPG GTYTVSVDAR
SRPSTADSFE IVIDGTVVGT FSPSQSYATY SISFTATSSS TRVEFRELAS QNSGEGVLID
NVRVVLGNPE FDDVLDGGEG NDTLDGAGGD DSLDGGTGTD SLIGGSGNDT LDGGADSDTL
DGGAGADSLR GGTGNDSLIG DTGNDTVDGG AGNDTLFGGQ GNDSLTGGTG NDRIFGDGPT
EGSATVTETR SVTPVTGADH TVLVWQLGQI TLNNAAGNDN PFENDTDGDS DVAGSTFTVN
LGASPVSIGL DDNDSAFNDG DTSQVLSQDS TINGISEDAG KRLTPEYAYS VQSSTGEVIN
IYAVELEGNR TVGFVTDKPL TVGETYTFLG RISTAPSVNY SNLATTWTTT TTTTAPIGND
TILGASGDTI FGGGGADTIV IDPTATNAAG TTLSGIQVDG GTTGTDSDRL DLTGYTFYRN
LVQTTDADGD STSGSVVVID AKGLARTVTF TEIETLLLPP PEPTNNGIVE GLETGETMDP
GYTDADGDQI DGTDGNDDRI EGRGGNDIIN AGLGNDSVTG GSGNDSIFGG LGNDSLDGGE
GSDSLAGGIG NDSLSGGLGD DDIAVGGADT ATGGSGDDVF VIDGTDTGSD VNITLDGGSD
GTSGAPDDAA NGDAGDLLDL SAGTSGLTVN LGANPENGTV NGLDSDGGID LTFTEIERLL
TGSGNDTING GSSTGPVSID TGSGNDTIAT GSGNDSITGG AGDDTISSGS GNDRVIGGSG
NDSVDGGGSD DTLQGNDGDD TLAGGDGNDS LDGGDNDDSL TGGTGNDTLV GGDGSDTLDG
GDNNDSLEGG SGEDDLTGGR GDDTLSGDGG NDTLAGGDGD DSVSGGTGND SLTGGDGNDT
LSGGTGTDTL QGGAGNDSLI GGDGDDDIVV GAGDIAQGGA GDDEFTVDPT LSGSAPITVI
GGETVEEAVI DPTNNPGGRI GDVLDLRGLS DVVVTYTNPD PISGTSENGT ATFRNTSGNL
VTLTFSEIEN VLTSADGIVD GTGAGDLMTP TSGPGGTPFR DPQGDQIDGT DGLNDRVAAG
AGNDTVDAGL GNDTVDGDIG NDSIAGGSGD DSLIGGSGND TLSGDAGNDL LDGGASDDSL
SGGADNDTLF GDAGRDTLAG GSGNDQLFGG DEADDLSGND GNDTLSGDGG NDTLDGGDGA
DRLDAGLGDD RIIGGEGADT IDAGQGDDSV SADGGNDFVG LGDGNDSAEG GTGNDTIGGG
EGNDSISGGG DADSLIGGAG NDTLDGGDGN DTLAGDDGSD LLTGGAGNDS LLGGANDDDL
IIGAGDRAEG GDGDDEFRVN PALSGNAGIT VIGGETGENL TDPTNGGSGD VLDLRGLTNV
ALSFTGAESG TATFQNSGGQ TVTITFAEIE RVLVDTNGIV DGTAAGDLMT PTSGVAGTPY
TDTQGDQIDG SDGLNDVVAA GQGNDTVDAG LGNDTVDGGA GDDSLSGNVG NDSLTGGEGA
DTLSGDDGAD LLDGGEGSDS LSGGDGNDSL FGADGTDTLL GGIGDDRLDG GEGSDSLAGG
TGADTLIGGS GADTLEGGAG ADSVTGGAGD DDIIVGGADT AAGGSGDDVF TADASDSNVN
AQIDGGSDAT SGNADDTANG DAGDQLDLSA QTSNITIDFS PANAENGTVN GLDGDGQTDL
TFTEIERFAT GSGNDTIDGA GTTGAILIAT NAGNDSIATG GGNDVIDAGS GNDTIAANSG
NDTVNAGSGD DVVNGGANDD VLDGGSGNDD LTGGAGEDLL IGGDGNDTLD GGSEDDTLTG
GIGDDRLIGG NGDDSLSGNE GRDTLQGGTG NDTLDGGDEA DSLQGGSGND RLFAGAGADI
AEGNEGDDLI EGGDGADTLF GNEGNDTLDG GDGADSLVGG DGRDSVTGGE GDDVINTRNT
QATPDEAGAL SDSDPNDDRD TVFGGAGNDT ILTGDDADLI QGEGGNDSID AGLDDDSVFG
GAGDDTIIGE EGDDLIEGAE GNDLLYGGSA ALTPGDLPND GTDPLTTNNE DTVLGGEGND
TIYGFDDNDS LSGDGGNDVI FGGLDDDRID GGAGNDSLSG DEGNDSLTGG EGNDTLNGGV
GRDTLVGGIG ADLLVGGAGA DLFTVQGADT ITDFDATTGI QGTPGAPTND NDFVDLSAFY
NDATLATFLQ NNPGATFSNP LAWLKADQAD GVLQGAGDLR LQNGGTAVDG ALLNVENTAV
VCFTRGTRIL TAEGERAIED LAPGDLVFTL DHGYQPIRWI GSSTVAGKGR FAPIVIEAGA
LGNTRRLAVS PQHRMLLSGW QAELLFDEPE VLVAAKLLVN DGSIRAEECE KVEYFHMLFD
AHEVVIAEGA PSESFHPGHV GWGALAEAAR EEILALFPQL DGMDFSAYGP SARRSLTAAE
ARVVRDALLA ETPIRAAE
//