ID A0A3T1CYC8_9BACL Unreviewed; 2716 AA.
AC A0A3T1CYC8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Big-1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=KCTCHS21_02100 {ECO:0000313|EMBL:BBI30811.1};
OS Cohnella abietis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2507935 {ECO:0000313|EMBL:BBI30811.1, ECO:0000313|Proteomes:UP000289856};
RN [1] {ECO:0000313|EMBL:BBI30811.1, ECO:0000313|Proteomes:UP000289856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS21 {ECO:0000313|EMBL:BBI30811.1,
RC ECO:0000313|Proteomes:UP000289856};
RA Jiang L., Kang S.W., Kim S., Jung J., Kim C.Y., Kim D.H., Kim S.W., Lee J.;
RT "Complete genome sequence of Cohnella hallensis HS21 isolated from Korean
RT fir (Abies koreana) rhizospheric soil.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000256|ARBA:ARBA00004237}.
CC -!- SIMILARITY: Belongs to the intimin/invasin family.
CC {ECO:0000256|ARBA:ARBA00010116}.
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DR EMBL; AP019400; BBI30811.1; -; Genomic_DNA.
DR KEGG; cohn:KCTCHS21_02100; -.
DR OrthoDB; 283370at2; -.
DR Proteomes; UP000289856; Chromosome.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003344; Big_1_dom.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR047589; DUF11_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR001434; OmcB-like_DUF11.
DR InterPro; IPR001119; SLH_dom.
DR NCBIfam; TIGR01451; B_ant_repeat; 2.
DR PANTHER; PTHR43308:SF4; OUTER MEMBRANE PROTEIN ALPHA; 1.
DR PANTHER; PTHR43308; OUTER MEMBRANE PROTEIN ALPHA-RELATED; 1.
DR Pfam; PF02369; Big_1; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF01345; DUF11; 4.
DR Pfam; PF00395; SLH; 2.
DR SMART; SM00634; BID_1; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49478; Cna protein B-type domain; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51127; BIG1; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022601};
KW Reference proteome {ECO:0000313|Proteomes:UP000289856};
KW S-layer {ECO:0000256|ARBA:ARBA00022601};
KW Secreted {ECO:0000256|ARBA:ARBA00022601}.
FT DOMAIN 1945..2048
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 2486..2549
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2550..2613
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2615..2673
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 2696..2716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2716 AA; 289446 MW; C56C5EE24BC6F700 CRC64;
MIRLKKHLSI LLSALLVLQL FSSLIGVGSV SASPGTPYIG SQIDFWVTGV NDTPQSKLRD
KQRGNPLAEL VLGVETEIVL HAKNKAAAGS GKTAYNVGLE LVLPDGIVLA SSESPSTLEP
QSDGSTIAFW KDIKDLAGNE EFEFPVKVKV TDNYLKKAPP AAVKYGDSLP IKSSLYASSD
ARQLYYEAIA PTSQVTTNVK VVPFSVRIIH DAKNVKGAGS DLTVPVGGAE WGELPYTVKI
INNTRDITTF SKFTQTVGGA LEVYGFAGAT TSAQTVSGSD RKIEWTGLSL TAGASKQLTF
KTAYFHKDIV SGVENQGAVI THGTERNISF AYTANVNGVT YTDDALHPVA AKSVSHDIVV
YKSVALPTGK STIGYGDVLK YTLTVKVNEY ESVSNVHVKD TIGDGQTFVK YISTPGTVAS
PTKSGGKTVL DWDLGTLSYS DAAKRQITLE YEVKVDNAWT AAHGEGPIVA NDVLVNDVEV
SGETVSSGVV KDSDYTEVYV GTPTINERIT MVNGGTIVRG SPVNPQTQSV TVGDNVDFHV
GYDAIGLQAK QHNVRIYDYL PLGTTLVGDP TSYVIDTIVP TYDPVQNLLI WDWAAVNRKI
NEGQLAELFK EIKVLVTDNT SSVKKDKGAK NLVKLSYENS DGIVESKRQE VKLVYEEPEV
IISRSVNKTT NLVGTDEVTI TLTLTNTGTT PAYHVKLTET VPTDLTTPQP FGSYTFTAVG
NVLSFAEVPQ INPGQSVIVQ YKANVINPIG AAREIVLEKA AWTYVGQNDT NIVHRTYNGL
ETTQTKLYAK SPVITKEVVD TSNDKNNLRV GDWVVYKVDV QVPANTIAYA PSVINEIPNN
ETLTNIYKNY DTSTHVGTIP VTATPVAGKV TINVPSPAAG DRYTYYYKTT VNRINPGAQE
DHQSDAWFEW NDDSSLSTPP HHHSISPVAK VTVTVKAPQL EITLSPNAAS MKKGDSAKQF
TATVRNKGKN TAYSFTPTAV LPAGFIFGAN PNNYNISGQT ISFGLVTSLA PNAEIAYTFN
AALDHVEGAG STKSITGNTG DYYSKDTDGT KYDYTIGTSA ITVPSVTITN AITATSSGDL
TKIRPGDTVD YQIIVTVPKG TQAFDLVVKD TLANLGNFDI VNKPQSLAAS GNILTATLEN
QDATLNEIVH TFNLQLRAKT DKFLVGDPTV YSTSAIAYWN TSSGVGPVQT APATTSITVV
QPVLGISAVA IAAPNKIFNN DNKEISVSFR LTNAGTSVAK NASVKVNLPV GVAVKTGTIS
DNGVLNGVGN EITWTGLSGS NQDVTFVVTS TTAVSPGSTL NINATLLSYN SRDAEPTKEY
TPNAQAQQVL TIAPVTATAS ITSTTNNSVT TVRPGDEVTY KLAINIPINT TTFNTRLDEL
TTLTGLTIIS VKPVGGSTIT PTAEHIFPLG DLVGALTPIE YEIVAKVRTD QSPNQNPYTA
TYTPILTYDS LKVSGTPKPV TVTALDISVA EPKLSLLLSG TKTQFDEADE TITYTLKVTN
GGQSPAFNPA LELTLPTGVH FVDVGSEAVV TVIGDGTVPS VHFTWAPGTI AAGAYKELVF
TASPDAATEV KKAFDIDFTL LQYFSLPNSG GKQYASLNSN KLNVTIEGAH LLNTAPDQRV
AAAQDATFEH TLTNTGAGAD TFDVSAVFPY SADVYVDGIK VIDNKSAVDA LLANIPLPPG
GTSTLKWVIH VPEGTPYDND NPQLINLEAK GIISLKSTLA TDKLYIVGSE LDGWTGSQAR
IGWTEPTFAP GDPIKLSATS SNDIQKLKAS YVYDGHTVDV LFTLDNPTTY VTDGYKIWSN
VFTRLPDDIL NGLGNSNSFQ VTFEGLSSTD AVIQTDDWSS ASTGANNAFT VRNSLIIKGL
ITDGSTAIGI PEAKVTLYNE DANHLLVATV TADTNGDYNF GQQKAARYSL VVEKEGYASG
QTQFFALASS ADTEIVVDVA LTAYKLALDA NPSTIVGDGH SQSRLTATIT DLEGNPVAGL
PVTFTAPPGK GSFPSGATAV TDANGKASVL FQSSQISGIL SERFPVTATA FDTSHNKLAQ
ANIIVTFEPA SIEGIVTEMV NGVAVPVSGA VVVISKDFDN DGVIDFTGTA VTGADGKYTI
AIPRGNVQYD LVITKPVQVG GHTENIAFQQ TVTAGNISGL GNDVFVPNKG ATGIILFSLS
GGGAGLLAPA LQSKLTVRLL DITSNAQVGA SEPLALNGTF SLKNVPQGSY KLELSYELAP
GRSIIVNGTV NGLPTVQVTQ GGELNIIQEL IDPYGKITDY DTNAPIEGAH VELYYADTPR
NILKGLVPNT PVSLPAIVGF APNDNASPQD SDAAGDYAFM VYDHTDYYLR VTKPGYHGYI
SPTISVELDI VRHDLTLSRI VSTGPSNGSG GGGTIPLPGQ RDLAAHLYSD KASYEEGSEI
TYTVVYTNKT NEIAHGVVVQ AEVPLFTSVS DAANGSVNGN LISWKIGDLP AGGKGTIVYK
VKVQATGLLK AEVRVDNTAT ITSTDNLINV DDDTSKLQVL LFSKRYAEQR HTRYILGYPD
GEFKSQRTIT RAEIAAIFAR LLDLRSTVTG AKLFPDVEPT FWAGGYIEAT VKAGLFSGYE
DKTFRPNNAI TRAELSQVIS KYLKLTAPAP ADLHFTDIGQ HWAKNAIEEI YRYHIISGYP
DGTFGPGRKM IRAEAVAMIN RLLFRGPLTQ TGQTFPDVSP SFWAFGDVEE SVKSHSYKRN
SDGSESMTEL IPEPIW
//
