ID   C5BHW7_TERTT            Unreviewed;      1213 AA.
AC   C5BHW7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=PT repeat/fibro-slime domain protein {ECO:0000313|EMBL:ACR12989.1};
GN   OrderedLocusNames=TERTU_1857 {ECO:0000313|EMBL:ACR12989.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12989.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR12989.1, 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).
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DR   EMBL; CP001614; ACR12989.1; -; Genomic_DNA.
DR   RefSeq; WP_015819102.1; NC_012997.1.
DR   AlphaFoldDB; C5BHW7; -.
DR   STRING; 377629.TERTU_1857; -.
DR   KEGG; ttu:TERTU_1857; -.
DR   eggNOG; COG0810; Bacteria.
DR   eggNOG; COG3291; Bacteria.
DR   HOGENOM; CLU_298947_0_0_6; -.
DR   OrthoDB; 9758386at2; -.
DR   Proteomes; UP000009080; Chromosome.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011874; Fibro_Slime.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   NCBIfam; TIGR02148; Fibro_Slime; 1.
DR   PANTHER; PTHR31137; PROTEIN PSIB-RELATED-RELATED; 1.
DR   PANTHER; PTHR31137:SF5; PROTEIN PSIQ-RELATED; 1.
DR   Pfam; PF18911; PKD_4; 3.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00089; PKD; 3.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 2.
DR   PROSITE; PS51820; PA14; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1213
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002948823"
FT   DOMAIN          1054..1213
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
FT   REGION          527..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..552
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..661
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..711
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1213 AA;  129350 MW;  93C9ECBACEB71E4D CRC64;
     MFQQFKLSLV RFSLVSSAVL LAACSGSDGE SQENMLQQDD NAIIADTQFV FISRNSEKTV
     DATADKLQKS LSSDTTTPLD VVAPYEFEPG AKLMLRSSLD IEGQSVDILA AYFGSPDYDV
     KNLNTSYDGK TLLFAAHGPL DHPTDNTWNI YEYRFETGEV RRLIADNVIA NAGQDTNPAY
     TKTQTIVFST DRAAGNPDHP SDVTLPEDTE ENCYKISPSE KPSLLHAMTL QGENIVQLTY
     GNHHDTQPAS LKDGRVAFMR WSRSYELVPQ CDLVLANTRS QTAAVNLFAS DYPAGIEAPA
     TWSNSELCAY TQDTPFGPAL ASNHYSILRI AADGSELQRL YNTVDTGASD EAMLNLQELV
     QAENGQLITL LKHRYNGFLG GNVMELQSPN DVASGVVFAN MALEPVIADS VGLFPNQASL
     PGWYSAVAPY RDGSSRLLVS WAQCTEVDAG VSAFCRADSD ANSIESAYGI WVYNPQTDSR
     LPVVKAKAGT EYTELALAQP HVGLDYPFAP YSDDYVEDVD GSRIVCDDPG VQPTPEPSVV
     PSYPPSPTPT PVPSVQPSVM PSVVPSIVPT IAPSVVPSVT PSVAPSITPT MTPSVVPSVT
     PSVTPSIVPS VTPSVAPTVA PTPTPSVTPS IAPPTPVPSS VPSVVPTPTA EPTPVPTAEP
     SVTPSAEPSI EPSVEPSAEP SVEPSVEPST EPSAEPSAEP TPTPTPSPSP VNHAPTADAG
     LDQALETGDV AQLNGSGSTD LDGDPLTYSW YFVELPVTSG VTLADETSVT PQFMPDVAGA
     YVVALVVSDG TSESDVDTVS INVSLANTAP VADAGDDLST SVGSSVSLDG SGSFDADGDA
     LTYSWSLVSA PAEAQVQLSD ASVMQPHVLV DTSGDYMFAL VVSDGLVESS ADMVVLSTSN
     AKPVADAGED RTVDQEGMLT VDGSGSYDPE MQPLAFSWSL ISTPDGSAAK LIAPESVATG
     IAVDLPGDYV VQLVVNDGEW NSEPDTVMIT VNEPPTCDMS GVDSRSFPVV IRDFKSSHPD
     FEYNIASDRG IVTEWLGEDG KPVYAHGRRG TETTNGPNAF ASWYNDVEDV NLRLPMSLEI
     QRTPGTDIWT YENSAFFPID DLGWGLTPGF EHNYHFTLES HLYFDYLGGE KFVFRGDDDL
     WLYINGRRAI DIGGVHGVQE KSIALDDVAD QLGIEIGGRY SFDLFFAERH TVESNFMFQT
     SIVLSCEEPE AHP
//