ID C7N333_SLAHD Unreviewed; 883 AA.
AC C7N333;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Putative collagen-binding protein {ECO:0000313|EMBL:ACV21554.1};
GN OrderedLocusNames=Shel_04940 {ECO:0000313|EMBL:ACV21554.1};
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:ACV21554.1, ECO:0000313|Proteomes:UP000002026};
RN [1] {ECO:0000313|EMBL:ACV21554.1, 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).
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DR EMBL; CP001684; ACV21554.1; -; Genomic_DNA.
DR RefSeq; WP_012797659.1; NC_013165.1.
DR AlphaFoldDB; C7N333; -.
DR STRING; 471855.Shel_04940; -.
DR KEGG; shi:Shel_04940; -.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_002287_0_1_11; -.
DR Proteomes; UP000002026; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00222; CollagenBindB; 3.
DR Gene3D; 2.60.40.1280; -; 1.
DR Gene3D; 2.60.40.740; -; 1.
DR Gene3D; 2.60.40.1140; Collagen-binding surface protein Cna, B-type domain; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008454; Collagen-bd_Cna-like_B-typ_dom.
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 Pfam; PF17961; Big_8; 1.
DR Pfam; PF05738; Cna_B; 3.
DR Pfam; PF05737; Collagen_bind; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17802; SpaA; 1.
DR SUPFAM; SSF49401; Bacterial adhesins; 2.
DR SUPFAM; SSF49478; Cna protein B-type domain; 4.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Collagen {ECO:0000313|EMBL:ACV21554.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..883
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002980719"
FT TRANSMEM 852..873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..254
FT /note="SDR-like Ig"
FT /evidence="ECO:0000259|Pfam:PF17961"
FT DOMAIN 286..392
FT /note="Collagen binding"
FT /evidence="ECO:0000259|Pfam:PF05737"
FT DOMAIN 445..508
FT /note="Prealbumin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17802"
FT DOMAIN 533..614
FT /note="CNA-B"
FT /evidence="ECO:0000259|Pfam:PF05738"
FT DOMAIN 621..705
FT /note="CNA-B"
FT /evidence="ECO:0000259|Pfam:PF05738"
FT DOMAIN 713..801
FT /note="CNA-B"
FT /evidence="ECO:0000259|Pfam:PF05738"
FT DOMAIN 838..875
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 38..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 94507 MW; 9F2D7E19D6D5EB1A CRC64;
MNTRKRGPRL VASLLSVLLA VNCLSVASLA FASEPLDSEE PAAVVQPVDG DTAVSTLETA
ESDEAEQSAA QDQPVGAEVE ADTDAAAAAA AEGDSRSQEA ADEQPKAEAS DASDANDEAV
TVQAEGTDDS AVVTLAVQNN VITSFEALLQ DGSGPVGNVS QWQVFRMKGN FELPNGQVHA
GDTTTITLPE KLKFNQTAAF DITDENGNVI GQAVIDGANK TVTITWTDFA ETHSDVSGDF
YFYVQIDRNM VDEAEDIPLN FDVSGNVVYG GDIHFIGIPD PAPYYMSKNG YQVQGKPRYI
HFQIPINTIG ADIQNAKLTD GVVNPGLTID ASSFRILEGT WVKIKGDWEL QNRTDVTSNY
TVQFSDDMRS FTLDMGTISA SQGFYVIYDT VASYDLVDGE VIRNDATFTG NGSELRHISA
TATYFEAGGS AVGYVYAINV RKVDEDGAAL AGAQFNVVRV ANGAVVGTIT TDASGNGSLS
GLLKDDYQLV ETVAPVGYTL LSEPVDVSAG SFDSNKTANV VVENSLERTS IPVSKVWVGP
AAGSVTMRLM ADGVETDSLV LSERNNWQGS FDDLPVYDPV DGHEITYLVT EDDVDGYSQE
FTVAEDGSYV FTNTNNEIVI VNGTKTWDDA DDQDGMRPES ITVRLLADGV EIMQDTVGAE
DDWSWEFAAL PKYDLVDNHE IAYTVTEDAV EGYSPEYNGF NVTNKHTPDK TSVTVVKAWD
DADNKDGIRP DQVTVRLLAN GEDTGKSVVL NAENNWEASF GDLDLKAGGT AIVYTVAEDE
VDGYTAVITG DAQTGFVITN THEPVVPPTP PSVEKPTDTP KDTPKDMPKK SVEQPKTKSK
AKPSIPKTGD DLAPGMLALG ALAVAGAGCL VWARRTKRNL QDR
//
