ID A8Y850_ECOLX Unreviewed; 1248 AA.
AC A8Y850;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 52.
DE SubName: Full=EspP beta {ECO:0000313|EMBL:CAM88667.1};
DE Flags: Fragment;
GN Name=espP {ECO:0000313|EMBL:CAM88667.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:CAM88667.1};
RN [1] {ECO:0000313|EMBL:CAM88667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=89/04 {ECO:0000313|EMBL:CAM88667.1};
RX PubMed=17704265; DOI=10.1128/AEM.00920-07;
RA Brockmeyer J., Bielaszewska M., Fruth A., Bonn M.L., Mellmann A.,
RA Humpf H.U., Karch H.;
RT "Subtypes of the plasmid-encoded serine protease EspP in Shiga toxin-
RT producing Escherichia coli: distribution, secretion, and proteolytic
RT activity.";
RL Appl. Environ. Microbiol. 73:6351-6359(2007).
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004571}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004571}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Periplasm
CC {ECO:0000256|ARBA:ARBA00004418}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AM691843; CAM88667.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Y850; -.
DR MEROPS; S06.002; -.
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: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 CDD; cd01343; PL1_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 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_dom.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR NCBIfam; TIGR01414; autotrans_barl; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..1248
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002730899"
FT DOMAIN 43..297
FT /note="Peptidase S6"
FT /evidence="ECO:0000259|PROSITE:PS51691"
FT DOMAIN 1020..1248
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAM88667.1"
FT NON_TER 1248
FT /evidence="ECO:0000313|EMBL:CAM88667.1"
SQ SEQUENCE 1248 AA; 135762 MW; 77B6279C6323FAF3 CRC64;
GLIAVSELSG RVSSRTTGKK KHKRILALCF LGLLPSSYSF ASQMDISNFY IRDYMDFAQN
KGIFQAGATN IEIVKKDGST LKLPEVPFPD FSPVANKGST TSIGGAYSIT ATHNTKNHHS
VATQNWGNST YKQTDWNTSH PDFAVSRLDK FVVETRGATE GADISLSKQQ ALERYGVNYK
GEKKLIAFRA GSGVVSVKKN GRITPFNEVS YKPEMLNGSF VHIDDWSGWL ILTNNQFDEF
NNIASQGDSG SALFVYDNQK KKWVVAGTVW GIYNYANGKN HAAYSKWNQT TIDNLKNKFS
YKVDMSGAQV ATIENGKLTG TGSDTTDIKN KDLIFTGGGD ILLKSSFDNG AGGLVFNDKK
TYRVNGDDFT FKGAGVDTRN GSTVEWNIRY DNKDNLHKIG DGTLDVRKTQ NTNLKTGEGL
VILGAEKTFN NIYITSGDGT VRLNAENALS GGEYNGIFFA KNGGTLDLNG YNQSFNKIAA
TDSGAVITNT STKKSILSLN NTADYIYHGN INGNLDVLQH HETKKENHRL ILDGGVDTTN
DISLRNTQLS MQGHATEHAI YRDGAFSCSL PAPMRFLCGS DYVAGMQNTE ADAVKQNGNA
YKTNNAVSDL SQPDWETGTF RFGTLHLENS DFSIGRNANV IGDIQASKSN ITIGDTTAYI
DLHAGKNITG DGFGFRQNIV RGNSQGETLF TGGITAEDST IVIKDKAKAL FSNYVYLLNT
KATIEKGADV TTQSGMFSTS DISVSGNLSM TGNPDKDNKF EPSIYLNDAS YLLTDDSARL
VAKNKASVVG DIHSTKSASI MFGHDESDLS QLSDRTSKGL ALGFLGGFDV SYRGSVNAPS
ASATMNNTWW QLTGDSALKT LKSTNSMVYF TDSANNKKFH TLTVDELATS NSAYAMRTNL
SESDKLEVKK HLSGENNILL VDFLQKPTPE KQLNIELVSA PKDTNKNVFK ASKQTIGFSN
VTPVITTQET DDKITWSLTG YNTVANKEAT QNAAALFSVD YKAFLNEVNN LNKRMGDLRD
INGEAGAWAR IMSGTGSASG GFSDNYTHVQ VGVDKKHELD GLDLFTGFTV THTDSSASAD
VFSGKTKSVG AGLYASAMFD SGAYIDLIGK YVHHDNEYTA TFAGLGTRDY STHSWYAGAE
VGYRYHVTED AWIEPQAELV YGSVSGKQFA WKDQGMHLSM KDKDYNPLIG RTGVDVGKSF
SGKDWKVTAR AGLGYQFDLL ANGETVLRDA SGEKRIKGEK DSRMLMSV
//
