ID A5GBS8_GEOUR Unreviewed; 2042 AA.
AC A5GBS8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Polymorphic outer membrane protein {ECO:0000313|EMBL:ABQ24965.1};
GN OrderedLocusNames=Gura_0756 {ECO:0000313|EMBL:ABQ24965.1};
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ24965.1, ECO:0000313|Proteomes:UP000006695};
RN [1] {ECO:0000313|EMBL:ABQ24965.1, ECO:0000313|Proteomes:UP000006695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ24965.1,
RC ECO:0000313|Proteomes:UP000006695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000698; ABQ24965.1; -; Genomic_DNA.
DR STRING; 351605.Gura_0756; -.
DR KEGG; gur:Gura_0756; -.
DR HOGENOM; CLU_231316_0_0_7; -.
DR OrthoDB; 262245at2; -.
DR Proteomes; UP000006695; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14256; Dockerin_I; 1.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00102; IPT; 1.
DR CDD; cd00603; IPT_PCSR; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR043772; MBG_3.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003368; POMP_repeat.
DR NCBIfam; NF041518; choice_anch_Q; 1.
DR NCBIfam; TIGR01376; POMP_repeat; 1.
DR PANTHER; PTHR34720:SF9; BLR4714 PROTEIN; 1.
DR PANTHER; PTHR34720; MICROCYSTIN DEPENDENT PROTEIN; 1.
DR Pfam; PF02415; Chlam_PMP; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF09136; Glucodextran_B; 3.
DR Pfam; PF18887; MBG_3; 1.
DR Pfam; PF01833; TIG; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00429; IPT; 2.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 3.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS50853; FN3; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006695};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..2042
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002683383"
FT DOMAIN 477..566
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 650..739
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 823..912
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 2042 AA; 199608 MW; EA1C050877586151 CRC64;
MSIRMTSAKI LRGRISFVAT LLCMVLTQPL SSFAASVTLD AADDVYTDSS RIPTAGYTTT
DMASVKDDSM SKIVNYVGRT PSISVLNGRT VVKFNLSGIS GAINSASFKF NVIDIHGTPI
LNLIKVTDNS WSEQPVGAST FPTYTDTDYI TQNSTPYSNQ SVTTGWNNIN VKDYIQEKIN
AGSPYVTIAM TGYATGATDD DFDFVSLNNG DALIPTLTVD YTPPPTVTGI SPSSGPVAGG
TSVTISGANF TSATAVTFGS TNATSYTVNS ATQITATSPA GSAGTVDITV TTAGGTSATG
ASDQFTYIAA PTVTSISPTS GPTDGSTSVT ITGTNFTGAT TVTIGGAAAT SVTVVNATTL
TATTPSGTAG VRDVVVTTPG GTGTGTGLFT YKASQTITFN SPGAQNFGTT PTLTAIASSG
LTPTFTSSTT GVCTITSGGA LTFATTGTCT INAGQAGDST YLAALPVSQS FSVAAVVPGA
PTIGTATAGD TQASVTFTAP ASNGGASITG YTATSNPGGV TGTCASSPCT VTGLTNGTAY
TFTVTATNSA GTGSASAASN SVTPAAAQTI TFNNPGAQNF GIAPTLTATA SSGLMVSFTS
STTGVCTVTA GGALTFVTAG TCTINADQAG NGSFTAAPMV TRSFAVNAVV PGAPTIGTAT
AGDTQASITF SAPASNGGAS ITSYTATSNP GGLTGTCASS PCTVTGLTNG TAYTFTVTAT
NSAGTGSASA ASNSVTPAAA QTITFNNPGA QNFGTSPTLT ATATSSLTVT FTSSTTGVCT
VTAGGALTFV TTGTCTINAD QAGNGSFLAA TTVSRSFTVI AVVPGAPTIG IATAGDTQAS
VAFTAPVSNG GASITGYTVT SNPGGLTSSG ASSPITVTGL TNGTAYTFTV TAHNSAGTGS
ASSASNSVTP NPGPTVVNVA VPANGIYKAG SNLDFTVTWD SAATVTGTPR IALLIGSAMV
YATYQSGSGT ASTLFRYTVL PGQTDTDGIT VGALSLNGGT IQNSSGTDAT LTLNSVASTV
NVLVDTTAPT LSSIATSNPT HSGGTLTATA NENALGSWIA VSSSATAPTV AQVLAGADYG
GVTVVAHGSG ALSAGSAVSF SLSGLVAATS YDIYLAAQDA AGNPSAAVSS ATLITTTTRV
VTTSSDSGPG SLRQTIADAN PGDIILFDPS LSGQTVTIAS PLVIAKDLSI GGYDARPITI
NGGGTTRIFQ VSGSTTFTLN YLTLTDGVAT DGGAISDNVN ATTFISLCTF SGNTATAAGG
AISAAGTMSI SDTLFAGNSA VQGGAIFNNN ALSLVNVTLA NNSANSGGGI YSSGGSTLVK
NTTIAGNNAT VQGGGIEIAS GAVGFRNSIV AGNTSPSGPD ISGFATSLGY NLVKDTSGAT
FTVTTGDLTG QDPLLGPLAD NGGPIKTMAL LLGSPAIDSG ACTGASATDQ RSMPRPQNGL
CDMGAYERGV PAALTATGGT PQSAAIDAAF ATPLKAKVTD SLGGVMEGIS VTFAGPGSGA
DITADGSVTT DAAGIASYGV TANGTAGAYT VTATVNALIA NFNLTNDKAN QAITFNPPAT
ATFGDAPIAL SATGGASGNP VIFSVASGPG SLNGATLTIT GAGNIVVTAS QAGNANYNAA
PQVIRNIAIG KGAATIALGS LNATYDGTAK AVTATTTPAG LAVIVTYGGS STPPTAAGSY
PVAATIDDAN YSGTATGTLV IAYSATPPVL TISTLADGSV TNNATLNVSG QATSINGITS
VTVNGAAVTL AADGTFSQAV TLQAGTNTVT TIATDNAGTT TTDSRTITLD TTAPVITITT
PADNSTLAAS SVTITGSVDK NATVQATANS GSPQSAAMTN NTFTVTLNLA GGSNTIVISA
TDLAGNSASV KRTIVSDTTK PTLAITNPSQ DITISEPALT ISGTVTDALT DVSVTITCDG
KTYTPQVVDG AFQQQLTFVM AKQYAITVTA TDQAGNSVTT QRNVIYALSS LPSGDINGDG
KVDIADALLA LQMAVGLITP TSAQLATGDV APLSNGKPAP DGAIDIADAM LILEKAVGML
TW
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