ID A0A172ZEB5_9BACL Unreviewed; 729 AA.
AC A0A172ZEB5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|SMART:SM00060};
GN ORFNames=AR543_06060 {ECO:0000313|EMBL:ANF95607.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95607.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF95607.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF95607.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP013023; ANF95607.1; -; Genomic_DNA.
DR RefSeq; WP_060532689.1; NZ_CP013023.1.
DR AlphaFoldDB; A0A172ZEB5; -.
DR STRING; 1616788.AR543_06060; -.
DR KEGG; pbv:AR543_06060; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000078148; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000078148};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..729
FT /note="Fibronectin type-III domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008005800"
FT DOMAIN 391..465
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|SMART:SM00060"
FT REGION 484..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 175
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 330
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 729 AA; 75878 MW; 9D430FA705622CC3 CRC64;
MKKIIPVFTA SLLTLSCAFA TGLAYGEGST TTASGPDQEV IVVYKNQEGK EAVLEQSVEV
QHEFATVPAV SATVSPADLN ELVQDPNIAY VERNVPFTIA DEQVVAQASA INTNEQSRWN
YQAEQPNLEW DKGYNGAGVK VAVVDSGIAP HPELTIAGGV STVDYTTSYT DDNGHGTHVG
GIIAARNGDG QVTGMAPGVQ LYAVKTMGSD GKGNLQDVLE GVDWAIQNHM DVINMSLGTE
YDSQLLHNML DQAYNSGILV VASAGNSGAG TDTVNYPAQY SSVIAVAAVD SNLNRGSFSS
TGPKVEVAAP GVGILSTYLN NGYAFMDGTS QAAPHVAAML AILKQKNPSE SIASLRSDLQ
KYAVDLGTAG RDNQYGYGFV TFKPQVDVTA PGEVKNLQLA AKGTDYLTFN WQNPADSDFA
KVNVYDEQNN RVKSVTGNVY SAANLTPDTS YTFRMKTVDV KGNESSGVTI SGRTAAVPAA
EITPAPASSQ PQPVTQPPAP QPTTVPAPAP TPAVSVPVVT TPPPTDQVAQ IPAGGGGGGG
GGGGGGGGIP RPAAPKVQTP APTATAPSTP AQKAQQQLNN AKSSGKAADF IKARFAAKDL
NNAEFNKQLN QLKQSLGIKD LPSKANLRAS VPVRISLQAS LKSSTYKYID KSSITADNIA
ILDGSGNAVS NVNLSVKFNR IFITAADGSF APNQTYTVII EKGVKGKTTA SSDQSTALTS
PLVMQFTTR
//
