TSH_ECOLX
ID TSH_ECOLX Reviewed; 1377 AA.
AC Q47692; Q6QE02; Q83WR9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Temperature-sensitive hemagglutinin tsh autotransporter;
DE EC=3.4.21.-;
DE AltName: Full=Autotransporter tsh;
DE Contains:
DE RecName: Full=Temperature-sensitive hemagglutinin tsh;
DE Contains:
DE RecName: Full=Temperature-sensitive hemagglutinin tsh translocator;
DE Flags: Precursor;
GN Name=tsh;
OS Escherichia coli.
OG Plasmid pAPEC-1, Plasmid pAPEC-O2-ColV, and Plasmid pYA3432.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=O78:K80:H9 / chi7122 / APEC; PLASMID=pAPEC-1;
RX PubMed=8132344; DOI=10.1128/iai.62.4.1369-1380.1994;
RA Provence D.L., Curtiss R. III;
RT "Isolation and characterization of a gene involved in hemagglutination by
RT an avian pathogenic Escherichia coli strain.";
RL Infect. Immun. 62:1369-1380(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=O78:K80:H9 / chi7122 / APEC; PLASMID=pAPEC-1;
RX PubMed=10858231; DOI=10.1128/iai.68.7.4145-4154.2000;
RA Dozois C.M., Dho-Moulin M., Bree A., Fairbrother J.M., Desautels C.,
RA Curtiss R. III;
RT "Relationship between the Tsh autotransporter and pathogenicity of avian
RT Escherichia coli and localization and analysis of the tsh genetic region.";
RL Infect. Immun. 68:4145-4154(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A2363 / APEC; PLASMID=pAPEC-O2-ColV;
RA Johnson T.J., Nolan L.K.;
RT "Putative virulence region of a ColV plasmid from an avian pathogenic
RT Escherichia coli (APEC).";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-531.
RC STRAIN=APEC13 / APEC;
RA Simoes R.C., Delicato E.R., Gaziri L.C.J., Vidotto M.C.;
RT "Cloning and characterization of the tsh gene from an avian pathogenic
RT Escherichia coli strain.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 53-60 AND 1101-1111, FUNCTION, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF SER-259.
RC STRAIN=O78:K80:H9 / chi7122 / APEC; PLASMID=pAPEC-1;
RX PubMed=9916089; DOI=10.1128/iai.67.2.772-781.1999;
RA Stathopoulos C., Provence D.L., Curtiss R. III;
RT "Characterization of the avian pathogenic Escherichia coli hemagglutinin
RT Tsh, a member of the immunoglobulin A protease-type family of
RT autotransporters.";
RL Infect. Immun. 67:772-781(1999).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF SER-259.
RC STRAIN=RW193; PLASMID=pYA3432;
RX PubMed=15385451; DOI=10.1128/iai.72.10.5548-5554.2004;
RA Kostakioti M., Stathopoulos C.;
RT "Functional analysis of the Tsh autotransporter from an avian pathogenic
RT Escherichia coli strain.";
RL Infect. Immun. 72:5548-5554(2004).
CC -!- FUNCTION: Contributes to the development of lesions and deposition of
CC fibrin in the avian air sacs. It can act both as an adhesin and as a
CC serine protease. Agglutinates erythrocytes while in contact with the
CC extracellular surface of the bacterial cells. Can adhere to purified
CC hemoglobin and bind with great efficiency to extracellular matrix
CC proteins. Cleaves casein and exhibits mucinolytic activity.
CC {ECO:0000269|PubMed:10858231, ECO:0000269|PubMed:15385451,
CC ECO:0000269|PubMed:8132344, ECO:0000269|PubMed:9916089}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 26 degrees Celsius for hemagglutination
CC activity.;
CC -!- SUBCELLULAR LOCATION: [Temperature-sensitive hemagglutinin tsh
CC autotransporter]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Temperature-sensitive hemagglutinin tsh]:
CC Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Temperature-sensitive hemagglutinin tsh
CC translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=The cleaved C-terminal fragment
CC (autotransporter domain) is localized in the outer membrane.
CC {ECO:0000250}.
CC -!- DOMAIN: Adhesive and proteolytic functions of tsh lie in different
CC domains of the protein.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent cleavage (By similarity).
CC {ECO:0000250}.
CC -!- PTM: The C-terminus is blocked. {ECO:0000305}.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
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DR EMBL; AF218073; AAA24698.1; -; Genomic_DNA.
DR EMBL; AY545598; AAT35241.2; -; Genomic_DNA.
DR EMBL; AY280856; AAP33781.1; -; Genomic_DNA.
DR PIR; I54632; I54632.
DR RefSeq; WP_001080137.1; NZ_WVUZ01000043.1.
DR RefSeq; WP_011402691.1; NC_007675.1.
DR RefSeq; YP_444132.1; NC_007675.1.
DR AlphaFoldDB; Q47692; -.
DR SMR; Q47692; -.
DR MEROPS; N04.001; -.
DR MEROPS; S06.003; -.
DR TCDB; 1.B.12.4.2; the autotransporter-1 (at-1) family.
DR PRIDE; Q47692; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Hydrolase; Membrane;
KW Periplasm; Plasmid; Protease; Secreted; Serine protease; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..52
FT /evidence="ECO:0000269|PubMed:9916089"
FT CHAIN 53..1377
FT /note="Temperature-sensitive hemagglutinin tsh
FT autotransporter"
FT /id="PRO_0000387610"
FT CHAIN 53..1100
FT /note="Temperature-sensitive hemagglutinin tsh"
FT /id="PRO_0000026982"
FT CHAIN 1101..1377
FT /note="Temperature-sensitive hemagglutinin tsh
FT translocator"
FT /id="PRO_0000026983"
FT DOMAIN 53..302
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1111..1377
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT ACT_SITE 259
FT /note="Charge relay system"
FT SITE 1100..1101
FT /note="Cleavage"
FT VARIANT 175
FT /note="G -> W (in strain: APEC13)"
FT VARIANT 183
FT /note="D -> G (in strain: APEC13)"
FT VARIANT 209
FT /note="Q -> K (in strain: A2363 and APEC13)"
FT VARIANT 326
FT /note="F -> S (in strain: A2363)"
FT VARIANT 422
FT /note="H -> Y (in strain: A2363)"
FT VARIANT 634
FT /note="G -> S (in strain: A2363)"
FT VARIANT 842
FT /note="A -> T (in strain: A2363)"
FT MUTAGEN 259
FT /note="S->A: Loss of proteolytic activity. No effect on
FT hemagglutination activity."
FT /evidence="ECO:0000269|PubMed:15385451,
FT ECO:0000269|PubMed:9916089"
FT MUTAGEN 259
FT /note="S->T: No effect either on extracellular secretion or
FT on hemagglutination activity."
FT /evidence="ECO:0000269|PubMed:15385451,
FT ECO:0000269|PubMed:9916089"
SQ SEQUENCE 1377 AA; 148227 MW; 237423644D9AE012 CRC64;
MNRIYSLRYS AVARGFIAVS EFARKCVHKS VRRLCFPVLL LIPVLFSAGS LAGTVNNELG
YQLFRDFAEN KGMFRPGATN IAIYNKQGEF VGTLDKAAMP DFSAVDSEIG VATLINPQYI
ASVKHNGGYT NVSFGDGENR YNIVDRNNAP SLDFHAPRLD KLVTEVAPTA VTAQGAVAGA
YLDKERYPVF YRLGSGTQYI KDSNGQLTQM GGAYSWLTGG TVGSLSSYQN GEMISTSSGL
VFDYKLNGAM PIYGEAGDSG SPLFAFDTVQ NKWVLVGVLT AGNGAGGRGN NWAVIPLDFI
GQKFNEDNDA PVTFRTSEGG ALEWSFNSST GAGALTQGTT TYAMHGQQGN DLNAGKNLIF
QGQNGQINLK DSVSQGAGSL TFRDNYTVTT SNGSTWTGAG IVVDNGVSVN WQVNGVKGDN
LHKIGEGTLT VQGTGINEGG LKVGDGKVVL NQQADNKGQV QAFSSVNIAS GRPTVVLTDE
RQVNPDTVSW GYRGGTLDVN GNSLTFHQLK AADYGAVLAN NVDKRATITL DYALRADKVA
LNGWSESGKG TAGNLYKYNN PYTNTTDYFI LKQSTYGYFP TDQSSNATWE FVGHSQGDAQ
KLVADRFNTA GYLFHGQLKG NLNVDNRLPE GVTGALVMDG AADISGTFTQ ENGRLTLQGH
PVIHAYNTQS VADKLAASGD HSVLTQPTSF SQEDWENRSF TFDRLSLKNT DFGLGRNATL
NTTIQADNSS VTLGDSRVFI DKNDGQGTAF TLEEGTSVAT KDADKSVFNG TVNLDNQSVL
NINDIFNGGI QANNSTVNIS SDSAVLGNST LTSTALNLNK GANALASQSF VSDGPVNISD
AALSLNSRPD EVSHTLLPVY DYAGSWNLKG DDARLNVGPY SMLSGNINVQ DKGTVTLGGE
GELSPDLTLQ NQMLYSLFNG YRNIWSGSLN APDATVSMTD TQWSMNGNST AGNMKLNRTI
VGFNGGTSPF TTLTTDNLDA VQSAFVMRTD LNKADKLVIN KSATGHDNSI WVNFLKKPSN
KDTLDIPLVS APEATADNLF RASTRVVGFS DVTPILSVRK EDGKKEWVLD GYQVARNDGQ
GKAAATFMHI SYNNFITEVN NLNKRMGDLR DINGEAGTWV RLLNGSGSAD GGFTDHYTLL
QMGADRKHEL GSMDLFTGVM ATYTDTDASA DLYSGKTKSW GGGFYASGLF RSGAYFDVIA
KYIHNENKYD LNFAGAGKQN FRSHSLYAGA EVGYRYHLTD TTFVEPQAEL VWGRLQGQTF
NWNDSGMDVS MRRNSVNPLV GRTGVVSGKT FSGKDWSLTA RAGLHYEFDL TDSADVHLKD
AAGEHQINGR KDSRMLYGVG LNARFGDNTR LGLEVERSAF GKYNTDDAIN ANIRYSF
