ID E6VWE5_PSEA9 Unreviewed; 2107 AA.
AC E6VWE5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=FecR protein {ECO:0000313|EMBL:ADU61351.1};
GN OrderedLocusNames=Daes_0326 {ECO:0000313|EMBL:ADU61351.1};
OS Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS (Desulfovibrio aespoeensis).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU61351.1, ECO:0000313|Proteomes:UP000002191};
RN [1] {ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA Hazen T., Woyke T.;
RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU61351.1, ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RX PubMed=24874683;
RA Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA Goodwin L., Shapiro N.;
RT "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL Genome Announc. 2:e00509-14(2014).
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DR EMBL; CP002431; ADU61351.1; -; Genomic_DNA.
DR RefSeq; WP_013513288.1; NC_014844.1.
DR STRING; 643562.Daes_0326; -.
DR KEGG; das:Daes_0326; -.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG4254; Bacteria.
DR HOGENOM; CLU_232299_0_0_7; -.
DR OrthoDB; 5444704at2; -.
DR Proteomes; UP000002191; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 10.
DR InterPro; IPR006860; FecR.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF04773; FecR; 1.
DR Pfam; PF00353; HemolysinCabind; 17.
DR PRINTS; PR00313; CABNDNGRPT.
DR SUPFAM; SSF51120; beta-Roll; 10.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 7.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 40..136
FT /note="FecR protein"
FT /evidence="ECO:0000259|Pfam:PF04773"
FT REGION 187..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2107 AA; 214565 MW; 0D53BBCF29B27207 CRC64;
MPEATQIGVV TIAYGTATAE GPDGIRELTP NSPVFADDVI TTKGGASAVE IKFSDGAILS
QGPNSAVVLD TYVFNPDQSA GEMTVKLLQG TFRSVTGEIV DMNPEGFSLE TPLATIGIRG
TTTGHRITPG QPESHVVVDF VDKPVVIRPI SGGPVAIITQ DGGMVSASPG GLSPVFMASQ
AELAQFEQLS SQSLQQSAPD PGNANDDNDE GDDGDQDQPD SQDGDGDQAG DGAGDGDGAG
DEAGEGEGTG EGEGEGGEGP GDPITQGQGQ GQGVGQNQGG VFDTGTGVGQ GQGQGQGQGL
GTPPPPKIAA PPPPPPPPPP PPPPPPPPPP PPPPPIEDEP AQAAVVTTLD LSEWGDNLTV
DLQASPPYYE TTGDQSSREE LVSTASTTYA IRTVYGDASH DNAIIGSAQG DSLYGGAGAN
AINGMCGNDF MTVGHYESES NSYHLGAISL DDIVSGGNGT DTLAFDGASG STPLDNVTSI
EYIQLGSSAV NIQTTPDALV DAGATLTLDG SLSSQVTFWA NNDTNSHFYL IGGSGDDYLK
GSGLADTLFG GAGNDCLSGL GGDDTIFGTG GGNDTLLGGD GNDRFSLGTD LTGSDEINGG
DGADSLYFTD NGTGSDELTN VTGIEHIILG NANTHIVYSP SETGTITING SAITAANTLN
YNGADATQYQ HIIGGAGSDS ITGGSGNDTL EGGAGADTLN GGSGVNMLSY ASSTAGVNVN
LSTNMASGGH ADGDVLTSGS FHGVIGGSGN DTLIGTRHNE RFEGGAGNDR IDGSGGADTG
AGIGVDTIMG GAGNDTIVIS TPVGAGSIYN GEAGTDTLEL QTTAIFTAAS VSGIEVIYFA
SAGKTATFGV AQMGAWTLST FDPGSASTLG ITGTAGNDVI DLTTLTLGTN WGLSGNVIAI
QAGLGDDLIR ASASAEYIAG GEGFDTLDYS GSTAGVSVNL QTASVAGGYA NNDSISGIAA
VIGSDFADTL AGSDDSTNAL YGGGGNDSFI MSTYLEAEDT VSGGDGTDTL TFTYNGGDVL
TNVTGIEHIT LGDAATTLVG HDTLADYLST FTLDATALSG GNNLDWDGTF IANFRQHVIG
SAASDTIVGG SSHDTLLGGA GKDWLEGGAG CDSLDGGGND ELQRELDIAS YENEEYAINA
NLFTGRVTGG GYTDTISGIE GIRGTTLGDT FVGDSGWVNL FFDGGGSDSY DGNSEHDPDE
DTGFDIVSYH YATAGITAIM NGTSGSVTLG GNVDTLTDID MIWATPYDDL LTGGEGDEEF
MPGEGDDVVD GGGSEDWDSV TYWALDSGVN VTWVTDHWQV TDPDVNWTDT LTNIEAIEGS
AGDDSFTGSN NNDHFSGWAG ADAFDGGNGM DTVSYEEDPA GEDGVTGVYV DLSNNTATDG
WGNTESLISI EAIEGSDFDD EILGSSGDNW LGGNDGDDKI NGMGGTDTLI GGDGDDTFFF
TTDPSEGTLV DGEDGTDTLA VNGTVDLRGI SEIVDIEVMD FGVESTATVH SGLINNRTWQ
MRAEEGWATL AVLLAPGDVL NLTGLTFDQW GEQSVITVTG DEGNESVQGS SKADRVDGDE
GNDTLYGFGG NDTLQGGLGD DALYGGDGDD LITPYGVDSN PGAGFDTIDG GAGTDTLTDS
GGIDFSQMTI SNIEVIQATD YVTFTFGHHQ VNGADYSILG SADSTILFKG SGGNDTMDLS
GLNVDAMDGD INVSLLGGDD FFIGSTGDDA VDGGAGDDTL QGLGGDDTLT GGEGADRFVY
AFGAAINQSI DGDRITDFTA SQDMILLTGD LADTPLNWHP ATNYDGVIVG EADDQPVLVF
DPQNNILWYD DKPQIDDDAY QGKVATFSGM GGGFSFNDIF ARNQTITNPG GQINWAGDET
ANTMLGTEYD ERIFGDNGND SLHGGQGDDT LIGGKGQDTF DGGTGNNTIS FNYDPSGVHV
DIDTGQATDG WGNAETFSNI QNAFGSAHDD ILRGDSGQNV LFGGEGNDLL AGMGGMDTLI
GAGGDDTFAF YGSSASPAEI MDFDPTMDKI GLYVEYFNFF SGGVFNADNF AYLNAASYEG
TGVTFGNGET SGLVYASVAD SATGMLYYDP DSATTGGEFC LAMVSEMGMI PEEDNNVTAE
SFVEVTM
//
