YFAL_ECOLI
ID YFAL_ECOLI Reviewed; 1250 AA.
AC P45508; P39441; P45506; P45507; P76468; P77487;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Probable autotransporter YfaL {ECO:0000303|PubMed:16522795};
DE Contains:
DE RecName: Full=Probable secreted autotransporter protein YfaL {ECO:0000303|PubMed:22344647};
DE Contains:
DE RecName: Full=Probable autotransporter YfaL translocator {ECO:0000303|PubMed:22344647};
DE Flags: Precursor;
GN Name=yfaL; Synonyms=yfaF, yfaJ, yfaK; OrderedLocusNames=b2233, JW2227;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-938.
RX PubMed=6087316; DOI=10.1073/pnas.81.14.4294;
RA Carlson J., Fuchs J.A., Messing J.;
RT "Primary structure of the Escherichia coli ribonucleoside diphosphate
RT reductase operon.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 925-1198.
RC STRAIN=K12 / EMG2;
RA Estep P., O'Keeffe T., Robison K., Church G.M.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1180-1250.
RC STRAIN=OV6;
RX PubMed=2834621; DOI=10.1111/j.1365-2958.1987.tb01932.x;
RA Hussain K., Elliott E.J., Salmond G.P.C.;
RT "The parD- mutant of Escherichia coli also carries a gyrAam mutation. The
RT complete sequence of gyrA.";
RL Mol. Microbiol. 1:259-273(1987).
RN [7]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [8]
RP PUTATIVE FUNCTION, SUBCELLULAR LOCATION, AND AUTOCLEAVAGE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16522795; DOI=10.1110/ps.051889506;
RA Marani P., Wagner S., Baars L., Genevaux P., de Gier J.W., Nilsson I.,
RA Casadio R., von Heijne G.;
RT "New Escherichia coli outer membrane proteins identified through prediction
RT and experimental verification.";
RL Protein Sci. 15:884-889(2006).
RN [9]
RP PROBABLE FUNCTION, AND BIOTECHNOLOGY.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=22344647; DOI=10.1128/aem.07004-11;
RA Ko H.J., Park E., Song J., Yang T.H., Lee H.J., Kim K.H., Choi I.G.;
RT "Functional cell surface display and controlled secretion of diverse
RT agarolytic enzymes by Escherichia coli with a novel ligation-independent
RT cloning vector based on the autotransporter YfaL.";
RL Appl. Environ. Microbiol. 78:3051-3058(2012).
CC -!- FUNCTION: Probably an autotransporter. {ECO:0000305|PubMed:16522795,
CC ECO:0000305|PubMed:22344647}.
CC -!- SUBCELLULAR LOCATION: [Probable autotransporter YfaL]: Periplasm.
CC -!- SUBCELLULAR LOCATION: [Probable secreted autotransporter protein YfaL]:
CC Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Probable autotransporter YfaL translocator]:
CC Cell outer membrane {ECO:0000269|PubMed:16522795}.
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. Finally, the mature
CC protein remains tightly associated with the bacterium (Probable).
CC {ECO:0000305}.
CC -!- PTM: An approximately 170 kDa protein is detected in the outer
CC membrane, while a C-terminal 55 kDa fragment is detected in whole
CC cells. The full-length putative autotransporter may be cleaved to
CC release the mature protein from the outer membrane; Pefabloc SC, a Ser-
CC Thr protease inhibitor prevents the appearance of the 55 kDa C--
CC terminal fragment. {ECO:0000305|PubMed:16522795}.
CC -!- BIOTECHNOLOGY: The 'passenger' domain (residues 29-785) can be replaced
CC by other sequences which can be targeted to the cell surface
CC (PubMed:22344647). {ECO:0000269|PubMed:22344647}.
CC -!- SEQUENCE CAUTION:
CC Sequence=K02672; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC75293.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16050.2; -; Genomic_DNA.
DR EMBL; K02672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U30459; AAA74094.1; -; Genomic_DNA.
DR EMBL; Y00544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G64993; G64993.
DR RefSeq; NP_416736.1; NC_000913.3.
DR RefSeq; WP_001220077.1; NZ_LN832404.1.
DR AlphaFoldDB; P45508; -.
DR SMR; P45508; -.
DR BioGRID; 4262133; 267.
DR IntAct; P45508; 6.
DR STRING; 511145.b2233; -.
DR MEROPS; U69.A11; -.
DR TCDB; 1.B.12.1.5; the autotransporter-1 (at-1) family.
DR PaxDb; P45508; -.
DR PRIDE; P45508; -.
DR EnsemblBacteria; AAC75293; AAC75293; b2233.
DR EnsemblBacteria; BAA16050; BAA16050; BAA16050.
DR GeneID; 946595; -.
DR KEGG; ecj:JW2227; -.
DR KEGG; eco:b2233; -.
DR PATRIC; fig|511145.12.peg.2322; -.
DR EchoBASE; EB2695; -.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_003013_0_0_6; -.
DR OMA; VFNNNQA; -.
DR PhylomeDB; P45508; -.
DR BioCyc; EcoCyc:EG12850-MON; -.
DR PRO; PR:P45508; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR CDD; cd01344; PL2_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR043990; AC_1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR013425; Autotrns_rpt.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003368; POMP_repeat.
DR Pfam; PF18883; AC_1; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02415; Chlam_PMP; 3.
DR Pfam; PF12951; PATR; 3.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 2.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR TIGRFAMs; TIGR02601; autotrns_rpt; 1.
DR TIGRFAMs; TIGR01376; POMP_repeat; 2.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Hydrolase; Membrane; Periplasm; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1250
FT /note="Probable autotransporter YfaL"
FT /id="PRO_0000002713"
FT CHAIN 29..696
FT /note="Probable secreted autotransporter protein YfaL"
FT /id="PRO_0000440027"
FT CHAIN 697..1250
FT /note="Probable autotransporter YfaL translocator"
FT /id="PRO_0000440028"
FT REPEAT 919..920
FT /note="1"
FT REPEAT 921..922
FT /note="2; approximate"
FT REPEAT 923..924
FT /note="3"
FT REPEAT 925..926
FT /note="4; approximate"
FT REPEAT 927..928
FT /note="5"
FT REPEAT 929..930
FT /note="6"
FT REPEAT 931..932
FT /note="7"
FT REPEAT 933..934
FT /note="8"
FT REPEAT 935..936
FT /note="9"
FT REPEAT 937..938
FT /note="10"
FT REPEAT 939..940
FT /note="11"
FT REPEAT 941..942
FT /note="12"
FT REPEAT 943..944
FT /note="13"
FT REPEAT 945..946
FT /note="14"
FT REPEAT 947..948
FT /note="15"
FT DOMAIN 980..1250
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 914..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..948
FT /note="15 X 2 AA approximate tandem repeats of [DTPE]-P"
FT COMPBIAS 919..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 28..30
FT /note="AAV -> RGRS (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="K -> Q (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..66
FT /note="LV -> PG (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> Q (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..434
FT /note="AG -> SA (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> R (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="E -> S (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="V -> M (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 923..924
FT /note="PP -> AT (in Ref. 4; K02672)"
FT /evidence="ECO:0000305"
FT CONFLICT 948..994
FT /note="PAYQPVLNAKVGGYLNNLRAANQAFMMERRDHAGGDGQTLNLRVIGG -> L
FT LTSRC (in Ref. 5; AAA74094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1250 AA; 131153 MW; 17F98C05E299FC95 CRC64;
MRIIFLRKEY LSLLPSMIAS LFSANGVAAV TDSCQGYDVK ASCQASRQSL SGITQDWSIA
DGQWLVFSDM TNNASGGAVF LQQGAEFSLL PENETGMTLF ANNTVTGEYN NGGAIFAKEN
STLNLTDVIF SGNVAGGYGG AIYSSGTNDT GAVDLRVTNA MFRNNIANDG KGGAIYTINN
DVYLSDVIFD NNQAYTSTSY SDGDGGAIDV TDNNSDSKHP SGYTIVNNTA FTNNTAEGYG
GAIYTNSVTA PYLIDISVDD SYSQNGGVLV DENNSAAGYG DGPSSAAGGF MYLGLSEVTF
DIADGKTLVI GNTENDGAVD SIAGTGLITK TGSGDLVLNA DNNDFTGEMQ IENGEVTLGR
SNSLMNVGDT HCQDDPQDCY GLTIGSIDQY QNQAELNVGS TQQTFVHALT GFQNGTLNID
AGGNVTVNQG SFAGIIEGAG QLTIAQNGSY VLAGAQSMAL TGDIVVDDGA VLSLEGDAAD
LTALQDDPQS IVLNGGVLDL SDFSTWQSGT SYNDGLEVSG SSGTVIGSQD VVDLAGGDNL
HIGGDGKDGV YVVVDASDGQ VSLANNNSYL GTTQIASGTL MVSDNSQLGD THYNRQVIFT
DKQQESVMEI TSDVDTRSDA AGHGRDIEMR ADGEVAVDAG VDTQWGALMA DSSGQHQDEG
STLTKTGAGT LELTASGTTQ SAVRVEEGTL KGDVADILPY ASSLWVGDGA TFVTGADQDI
QSIDAISSGT IDISDGTVLR LTGQDTSVAL NASLFNGDGT LVNATDGVTL TGELNTNLET
DSLTYLSNVT VNGNLTNTSG AVSLQNGVAG DTLTVNGDYT GGGTLLLDSE LNGDDSVSDQ
LVMNGNTAGN TTVVVNSITG IGEPTSTGIK VVDFAADPTQ FQNNAQFSLA GSGYVNMGAY
DYTLVEDNND WYLRSQEVTP PSPPDPDPTP DPDPTPDPDP TPDPEPTPAY QPVLNAKVGG
YLNNLRAANQ AFMMERRDHA GGDGQTLNLR VIGGDYHYTA AGQLAQHEDT STVQLSGDLF
SGRWGTDGEW MLGIVGGYSD NQGDSRSNMT GTRADNQNHG YAVGLTSSWF QHGNQKQGAW
LDSWLQYAWF SNDVSEQEDG TDHYHSSGII ASLEAGYQWL PGRGVVIEPQ AQVIYQGVQQ
DDFTAANRAR VSQSQGDDIQ TRLGLHSEWR TAVHVIPTLD LNYYHDPHST EIEEDGSTIS
DDAVKQRGEI KVGVTGNISQ RVSLRGSVAW QKGSDDFAQT AGFLSMTVKW
