ID A0A1I5E4D3_9CLOT Unreviewed; 2420 AA.
AC A0A1I5E4D3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=LPXTG-motif cell wall anchor domain-containing protein {ECO:0000313|EMBL:SFO06193.1};
GN ORFNames=SAMN04488695_11341 {ECO:0000313|EMBL:SFO06193.1};
OS Proteiniclasticum ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Proteiniclasticum.
OX NCBI_TaxID=398199 {ECO:0000313|EMBL:SFO06193.1, ECO:0000313|Proteomes:UP000181899};
RN [1] {ECO:0000313|EMBL:SFO06193.1, ECO:0000313|Proteomes:UP000181899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML2 {ECO:0000313|EMBL:SFO06193.1,
RC ECO:0000313|Proteomes:UP000181899};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000256|ARBA:ARBA00007257}.
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DR EMBL; FOVK01000013; SFO06193.1; -; Genomic_DNA.
DR RefSeq; WP_074912763.1; NZ_FOVK01000013.1.
DR STRING; 398199.SAMN05421804_101695; -.
DR OrthoDB; 3194789at2; -.
DR Proteomes; UP000181899; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.1280; -; 1.
DR Gene3D; 2.60.40.740; -; 5.
DR Gene3D; 2.60.40.10; Immunoglobulins; 14.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008456; Collagen-bd_dom.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041033; Prealbumin-like.
DR InterPro; IPR041171; SDR_Ig.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR36108:SF13; COLOSSIN-B; 1.
DR PANTHER; PTHR36108; COLOSSIN-B-RELATED; 1.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF05737; Collagen_bind; 4.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17802; SpaA; 14.
DR SUPFAM; SSF49401; Bacterial adhesins; 6.
DR SUPFAM; SSF49478; Cna protein B-type domain; 10.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000181899};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2394..2412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 210..294
FT /note="SDR-like Ig"
FT /evidence="ECO:0000259|Pfam:PF17961"
FT DOMAIN 320..450
FT /note="Collagen binding"
FT /evidence="ECO:0000259|Pfam:PF05737"
FT DOMAIN 471..579
FT /note="Collagen binding"
FT /evidence="ECO:0000259|Pfam:PF05737"
FT DOMAIN 756..883
FT /note="Collagen binding"
FT /evidence="ECO:0000259|Pfam:PF05737"
FT DOMAIN 900..1031
FT /note="Collagen binding"
FT /evidence="ECO:0000259|Pfam:PF05737"
FT DOMAIN 1067..1123
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1167..1223
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1253..1318
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1348..1413
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1440..1508
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1537..1604
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1631..1696
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1725..1792
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1820..1886
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 1914..1979
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 2007..2072
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 2102..2166
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 2193..2260
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 2287..2353
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 2379..2418
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 587..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2420 AA; 264725 MW; 619B6164C4D71901 CRC64;
MRITLRRVSA LLLAMILLLQ SVFTIPVEVH GDAVGEESLI RAAYVTDLDK NLTKSMKAGG
EYLLALDMTM TLQEGEEKSN LTLALPDFFA PENLTDLEAA LQISFENGKL NFSISGDESF
EGILHIPFKV TGEDKEGTAV LDLTDEGYVL SFVPAPMEEE KDREEALSLP EESASLSTVE
EDFRFIEIQF TDEAGNIFSA DNPYSIDGKE TGKIQFTFHL LEGHEVKAGD TMSFPLPKEL
KPVTATSGLL GDIGTWTVST DGLVNFLFNE NVDGDDVQGS FFFRVFLDEE EMDETVEQVI
EFEGYPDFTL KFPVSPKGGT AIDKKGTINR EGWNATEAYW SVDINTALLK MVDPVVTDVM
PNHMMFKEGS LVVRTLEMNA KGERTPGEIL DPSLYTLEMV SGNPKIILHG LKEEELQRAY
RLEYTTTIQE PSEGFSGVQV FKNKAQLISD GKMNTAEATV SSGYGDALKK KSPVYDSVNQ
QLKWEIEYNY NEKNIPMDVA YLTDTWTPAG VMNLVNDSLF VYPVDIDEEG NASPSEIPLS
HELYELTYTP GAGFRLQFLQ DVEGQAYVIR YKTQLVNTSG DPIITGSGTV NNKVETGQGK
ESSGSGGYGQ QGLVKRRVGT DVGKKEIRFE VVINRNGYVM ENLVLTDQFT GDGLTLLEDT
VLIKDSSNVT LVEGTDYKLV YTAPAGSAPG SFKIEFLRTI DKQLTLTYTT HFERNSDDTA
TYRNTAGISW KYDGKDYTIG GISVNTTPSG HTAKNGVKNG SYNAVEKKIT WSIHTNYARL
PIGNPYTISD ALDASQEYVT DSLSVFTYEV NGAGGIINEK ILASELYQVV YPSEGNGNRI
TVSLVGQEGE RTAVGIRFKT QFKNELISEP SVRNSATFQS GETSFGLNAT VNIPYGGKLA
DKKGVQAGAF NERADWTVYL NPTQSKLTDY VLTDSPDLNS VLLKETFEVV LGVVDINGNI
TKSTTVLEKD KDYTLEFYSD PVTGNERFEL SFPNEITEAY VLSYSSYIDP LAPQGEAIKN
AYTATGKNVQ EDVSGGSSSE IVKKNDGGGT GTSVRGGLTL TKISEEEVLL SGARFGLYTS
DKKQLLREAV TDENGVLTFG GLRRGKYVLK ELKAPTGYVI SDELANGIDV ILDHTEDGEM
KILSFINEKT KATIRKITSA GALIASEAMF DLYKADGTLY VQNLKTVDGV IHLEDLPEGR
YYVVETQAPE GYIRNTAKHY FDIRIEENGT QVKPVVDVRN YKASVVLKKS DKNGVGLSGA
VFSLLNSEGS VLRANLSVNA QGVLRVNNLS PGTYELLETK APTGYLLNRV GLVFTIPEMV
EGAPKDFNLG NYINYKGAAR LYKTDAAKNP LQGAVFKVVD EKGVTVQENL ISGADGRVHA
LNLSPGRYSF VETKAPAGYV LDRTPKTFVI PESEIGEPAV VVAGDRINYK GSVRMMKVSE
NGNPLSGAVF ALHEILGGVS VKVGEYTSTS MGLVTAGNLA PGSYEFIEMK APEGYIINEE
PVAFAISDEA EGEPLQVNAG EAVNYKGSVL LTKLGEEEAR LEGAEFSLYQ EGVEEALMEG
LVTDEAGELI LLDLSPGEYY FLETKAPAGY IRNLEPLYFS IQQTDAGAPE RVSVSMENHK
GSALLQKENS EGEALRGAVF ALYKESGDVV LENITSDEEG VVRMGSLEPG KYLLKETKAP
EGYLLNTKTV AFSISESVEG VPEALHLGSF INYLGSAELV KTNEKDEPLT GAVFELRDEE
GVEVLVEGLT TDEEGKVRLT DLTPGTYGLY EVEAPKGYLR NLEPVLFTIP EKTEGEPETV
LVGPFVNHKG AAVLKKVDEE GYGLTGAEFA LYDEEGLLLQ EGLVSDEEGE VLIKELSPGT
YVLKEVQSPE GYLLNLTEIT FTIEDTYEGT VDVLHLDDYT NYLGSAYLMK TDHEGNALSG
ATFDVVSEEG ERVREDLRSD ENGKVLAIGL APGKYYFEET KAPEGYLKNT EKVNFTIASS
EEGAPEAVDA GSLVNYKGSA VLRKTAEDGT GLKDAEFALY SEEGFLVREN LTTDEEGSLR
LKELSPGSYW LEETKAPEGY IRNIDRVSFE IPMEAEGEPV ALTLDEFINW QGSVLLQKSD
ERGNPLEGAV FALRKDDVTI KELTTDALGQ ILVEGLTPGG YEFIEISAPT GFILDPTLHE
FRISEDAAGE PERILVGTLM NHQGKIVLEK TDEKGAPLAG AVFELRDQEG NLIHKELVSD
EEGKVKAEGL FPGSYVLKET SAPAGYIRNE QTLEFTVTEE HFGAPDVLDL GQFVNYQGSL
LLKKVDEDGQ PLQGAEFELK YLPDEGESIL LVSDENGFIK VEDLAPGRYT IEEIKAPEGY
TRNEEVFAFT ILESSPVKPD PVEMTVVNTL EFDDTEGQSP GDELPATGES ENEVFIPLLG
TMLVLAGVFH LMRRKKEKTS
//
