ID C5BQP5_TERTT Unreviewed; 672 AA.
AC C5BQP5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Trypsin domain lipoprotein {ECO:0000313|EMBL:ACR11425.1};
GN OrderedLocusNames=TERTU_3388 {ECO:0000313|EMBL:ACR11425.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR11425.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR11425.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP001614; ACR11425.1; -; Genomic_DNA.
DR RefSeq; WP_015817537.1; NC_012997.1.
DR AlphaFoldDB; C5BQP5; -.
DR STRING; 377629.TERTU_3388; -.
DR KEGG; ttu:TERTU_3388; -.
DR eggNOG; COG4886; Bacteria.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_408777_0_0_6; -.
DR OrthoDB; 5291933at2; -.
DR Proteomes; UP000009080; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF18884; TSP3_bac; 1.
DR Pfam; PF02412; TSP_3; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 2.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Lipoprotein {ECO:0000313|EMBL:ACR11425.1};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..672
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002948831"
FT DOMAIN 41..276
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 554..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 71200 MW; 6626D9AE2354B8E6 CRC64;
MKSRFAFLSA LLLLTLGAHT SRAAVKPDHP RSQSPEIVPY IVGGGNAEAG AWGFTVALMR
NASSPFEGYT CTGTLIGPDV VLTAAHCVEN ASTESLQVYA GSYDLNNRNG DGQLIDVRKI
RIHEEYNTRT LVNDIAVVFL AEPVDLPTVK LISAQALAAL VPGTRLSVAG WGSTRPVGDR
YSPTLKSVDV NYVDNATCNT AFEDAVTDEM MCAGVAEGGK DACDGDSGGP LVMELDGTRY
QVGIVSSGAS ECGQAGFYGV YTRLSVMDSW LEKAVTELIT LNTVDDQNLQ ACIEQTALSR
GWTRVDEVSE VVCENANITS LDGLAVYTQL RTLGLAGNPL QDLTVLPELS NLQQLDLANT
AIADLGTLAE MPWLSSVTLS GLDHITCVDV NSGPYSYGEL ADAACFNNVL GIELADAALA
SCIRNIVLED GVTAPDQIEL VNCSNKGVAS LQGLQAFTGL RSLHVLGGQI SDVSPLSNLV
ELRQLTLFAN NVSDLSPLAG LVNLYWLDIS DNQVSDLSPL VNLVNLSAFF IEGNSGITCM
PVSGRQLAYD DIPASCFSTE PTPDPEEIDS DGDGIIDAED NCPGRANPGQ RNSDDDERGD
ACDHDDDNDG FSDRAERDAG SNPLNPYSTP ETIHQDADGD GILDAEDNCP LVYNPGQVDR
DGDGIGNACD AR
//
