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Database: UniProt
Entry: C7N201_SLAHD
LinkDB: C7N201_SLAHD
Original site: C7N201_SLAHD 
ID   C7N201_SLAHD            Unreviewed;       845 AA.
AC   C7N201;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Putative collagen-binding protein {ECO:0000313|EMBL:ACV23442.1};
GN   OrderedLocusNames=Shel_24340 {ECO:0000313|EMBL:ACV23442.1};
OS   Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS   RHS 1) (Peptococcus heliotrinreducens).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV23442.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV23442.1, ECO:0000313|Proteomes:UP000002026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC   {ECO:0000313|Proteomes:UP000002026};
RX   PubMed=21304663; DOI=10.4056/sigs.37633;
RA   Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA   Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA   Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA   Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT   1).";
RL   Stand. Genomic Sci. 1:234-241(2009).
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000256|ARBA:ARBA00007257}.
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DR   EMBL; CP001684; ACV23442.1; -; Genomic_DNA.
DR   RefSeq; WP_012799540.1; NC_013165.1.
DR   AlphaFoldDB; C7N201; -.
DR   STRING; 471855.Shel_24340; -.
DR   KEGG; shi:Shel_24340; -.
DR   eggNOG; COG4932; Bacteria.
DR   HOGENOM; CLU_337039_0_0_11; -.
DR   Proteomes; UP000002026; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.3050; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR026588; Choice_anch_A.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041033; Prealbumin-like.
DR   InterPro; IPR022464; Strep_pil_isopept_link.
DR   InterPro; IPR038174; Strep_pil_link_sf.
DR   NCBIfam; TIGR04215; choice_anch_A; 1.
DR   NCBIfam; TIGR03786; strep_pil_rpt; 1.
DR   PANTHER; PTHR36108:SF13; COLOSSIN-B; 1.
DR   PANTHER; PTHR36108; COLOSSIN-B-RELATED; 1.
DR   Pfam; PF12892; FctA; 1.
DR   Pfam; PF20597; pAdhesive_15; 1.
DR   Pfam; PF17802; SpaA; 2.
PE   3: Inferred from homology;
KW   Collagen {ECO:0000313|EMBL:ACV23442.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..845
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002980693"
FT   TRANSMEM        809..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          172..433
FT                   /note="Choice-of-anchor A"
FT                   /evidence="ECO:0000259|Pfam:PF20597"
FT   DOMAIN          457..520
FT                   /note="Prealbumin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF17802"
FT   DOMAIN          547..668
FT                   /note="Streptococcal pilin isopeptide linker"
FT                   /evidence="ECO:0000259|Pfam:PF12892"
FT   DOMAIN          716..758
FT                   /note="Prealbumin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF17802"
FT   REGION          63..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..135
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  90173 MW;  ED16389D211D1A7D CRC64;
     MFRGRTYKLI ACVCAFSLCL IGLEPAFQAY AYDEAEIVEG STVEIESDEE SVYALAEATD
     TLTVPSEDSV ASESESELES EYEDSEEDAA SEESEIVDDE TAADDEGTTL ESEEAVDEEA
     AVEEAAPEEE EAQAAIDETP VLRAAPAKAP ARAPTSNARM PEEGYTLEYL ANRGYSLVCF
     ENATIDQHTM GGLLIGGDMT QTTSAPGIAD SQYVAAPSYI EGYARPIDTG VFNARSRQNP
     VQPLYVSSRN TVSPDGKMLN GVGNSVSGEG YNYHGQVVVN DGYVDWAKME KAATSLSRQL
     KDVSSVTLNE FQDWSEVPID AGTSVTFENT GAKHVKVNVK GSSKKFTVIN ILDSGTVYAP
     QVISYNGRQL STAEDGEDMP IILNFPNATK VVIGDQTPEQ GHIIAPNAYV EINGGNYNGT
     IICKSAKLSG QGHVRRFHGD YPGPALQPVW ISKADSQETP LAGATLEIVD KNGEVVDSFV
     TTDEPYGLKV LPGTYTLREK DVPAGYQKAE DIAFEVSDKG VITVDGVQVA DKTVTMTDEF
     NPVTANLQAH KTLKGGQLKG DDFQFVLKDQ AGEEVETVKN DAQGFVQFSP MTFDEPGTWT
     YTISEVDGSF TDAADCGGMA YDANVYTAVV DVAKGENGLE ANVTYKDASG NPVAVGDANS
     DGAPVFVNVQ VQSLELHKVD GTDRPFPSDL NALVAFDVSY TSPEGATEVV QSGIHPDAQG
     IVKFSNLKPG TYTITETDAP DSYIKLEEPI VVTVTSEGAI ELTSAQENVV SLVDAVNADS
     TAQAAPGKVL MVRNYPYIVM PETGLSNRLV FQTLGAIAML VGACLYATTR RRARGSSPKG
     GCDGI
//
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