PIPB2_SALTY
ID PIPB2_SALTY Reviewed; 350 AA.
AC Q8ZMM8; Q6QNB4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Secreted effector protein PipB2;
DE AltName: Full=Type III effector PipB2;
GN Name=pipB2; OrderedLocusNames=STM2780;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, REGULATION BY
RP SSRA/SSRB, SIMILARITY, AND SUBCELLULAR LOCATION.
RC STRAIN=SL1344;
RX PubMed=12864852; DOI=10.1046/j.1365-2958.2003.03598.x;
RA Knodler L.A., Vallance B.A., Hensel M., Jaeckel D., Finlay B.B.,
RA Steele-Mortimer O.;
RT "Salmonella type III effectors PipB and PipB2 are targeted to detergent-
RT resistant microdomains on internal host cell membranes.";
RL Mol. Microbiol. 49:685-704(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, FUNCTION OF C-TERMINAL DOMAIN, REGULATION, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF THR-340; LEU-341; PHE-342; ASN-343; GLU-344; PHE-345 AND
RP TYR-346.
RC STRAIN=SL1344;
RX PubMed=15987736; DOI=10.1091/mbc.e05-04-0367;
RA Knodler L.A., Steele-Mortimer O.;
RT "The Salmonella effector PipB2 affects late endosome/lysosome distribution
RT to mediate Sif extension.";
RL Mol. Biol. Cell 16:4108-4123(2005).
RN [4]
RP REGULATION BY SLYA AND PHOP/PHOQ.
RC STRAIN=ATCC 14028s / SGSG 2262, and LT2 / SGSC1412 / ATCC 700720;
RX PubMed=15813739; DOI=10.1111/j.1365-2958.2005.04553.x;
RA Navarre W.W., Halsey T.A., Walthers D., Frye J., McClelland M.,
RA Potter J.L., Kenney L.J., Gunn J.S., Fang F.C., Libby S.J.;
RT "Co-regulation of Salmonella enterica genes required for virulence and
RT resistance to antimicrobial peptides by SlyA and PhoP/PhoQ.";
RL Mol. Microbiol. 56:492-508(2005).
RN [5]
RP FUNCTION, FUNCTION OF THE C-TERMINAL PENTAPEPTIDE DOMAIN, AND SUBUNIT.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023, and SL1344;
RX PubMed=16938850; DOI=10.1073/pnas.0605443103;
RA Henry T., Couillault C., Rockenfeller P., Boucrot E., Dumont A.,
RA Schroeder N., Hermant A., Knodler L.A., Lecine P., Steele-Mortimer O.,
RA Borg J.-P., Gorvel J.-P., Meresse S.;
RT "The Salmonella effector protein PipB2 is a linker for kinesin-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13497-13502(2006).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. Involved in the
CC reorganization of late endosome/lysosome (LE/Lys) compartments in
CC mammalian cells. Necessary and sufficient to link kinesin-1 onto the
CC Salmonella-containing vacuole (SCV) membrane. Required for centrifugal
CC extension of lysosomal glycoprotein-rich membrane tubules, known as
CC Salmonella-induced filaments (Sifs), away from the SCV and toward the
CC cell periphery. Required for virulence, but not for intracellular
CC survival and replication in phagocytic cells.
CC {ECO:0000269|PubMed:12864852, ECO:0000269|PubMed:15987736,
CC ECO:0000269|PubMed:16938850}.
CC -!- SUBUNIT: Interacts with the host kinesin light chain (KLC), a subunit
CC of the kinesin-1 motor complex. {ECO:0000269|PubMed:16938850}.
CC -!- INTERACTION:
CC Q8ZMM8; Q07866: KLC1; Xeno; NbExp=4; IntAct=EBI-15598815, EBI-721019;
CC -!- SUBCELLULAR LOCATION: Secreted. Host membrane. Note=Secreted via the
CC type III secretion system 2 (SPI-2 TTSS), and delivered into the host
CC cell. In phagocytic cells localizes to the Salmonella-containing
CC vacuole (SCV) and tubular extensions from the SCV, Salmonella-induced
CC filaments (Sifs). In epithelial cells localizes to peripheral vesicles,
CC in addition to SCVs and Sifs. Concentrates in detergent-resistant
CC microdomains (DRMs), present on the intracellular membranes of SCVs and
CC Sifs.
CC -!- INDUCTION: Expression of the gene is regulated by the two-component
CC regulatory system SsrA/SsrB. It is also activated by SlyA and
CC controlled by the two-component regulatory system PhoP/PhoQ.
CC -!- DOMAIN: Contains various tandem pentapeptide repeats in the C-terminal
CC region. The pentapeptide motif is required to efficiently recruit
CC kinesin-1. No position is completely conserved in these repeats, whose
CC consensus sequence is A-[DN]-[FLM]-X-X. The C-terminal 38 amino acid
CC residues, specifically, the C-terminal motif LFNEF, are required for
CC peripheral localization of PipB2 and redistribution of lysosomal-
CC associated membrane protein (LAMP). The N-terminal 225 amino acid
CC residues are sufficient for type III translocation and association with
CC Sifs and SCVs, but not accumulation in peripheral vesicles.
CC {ECO:0000269|PubMed:12864852}.
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DR EMBL; AY532917; AAS66036.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21665.1; -; Genomic_DNA.
DR RefSeq; NP_461706.1; NC_003197.2.
DR RefSeq; WP_001738474.1; NC_003197.2.
DR PDB; 2LEZ; NMR; -; A=17-161.
DR PDBsum; 2LEZ; -.
DR AlphaFoldDB; Q8ZMM8; -.
DR BMRB; Q8ZMM8; -.
DR SMR; Q8ZMM8; -.
DR DIP; DIP-61260N; -.
DR IntAct; Q8ZMM8; 3.
DR STRING; 99287.STM2780; -.
DR PaxDb; Q8ZMM8; -.
DR EnsemblBacteria; AAL21665; AAL21665; STM2780.
DR GeneID; 1254303; -.
DR KEGG; stm:STM2780; -.
DR PATRIC; fig|99287.12.peg.2931; -.
DR HOGENOM; CLU_067808_0_0_6; -.
DR OMA; ADCDGAN; -.
DR PhylomeDB; Q8ZMM8; -.
DR BioCyc; SENT99287:STM2780-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR InterPro; IPR001646; 5peptide_repeat.
DR Pfam; PF00805; Pentapeptide; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Host membrane; Membrane; Reference proteome; Repeat;
KW Secreted; Virulence.
FT CHAIN 1..350
FT /note="Secreted effector protein PipB2"
FT /id="PRO_0000278299"
FT DOMAIN 162..201
FT /note="Pentapeptide repeat 1"
FT DOMAIN 202..241
FT /note="Pentapeptide repeat 2"
FT DOMAIN 247..286
FT /note="Pentapeptide repeat 3"
FT DOMAIN 287..326
FT /note="Pentapeptide repeat 4"
FT MUTAGEN 340
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:15987736"
FT MUTAGEN 341
FT /note="L->A: Prevents the peripheral accumulation of GFP-
FT PipB2 and LAMP-1. Slightly affects its LE/Lys
FT redistribution."
FT /evidence="ECO:0000269|PubMed:15987736"
FT MUTAGEN 342
FT /note="F->A: Partial reduction in the peripheral
FT accumulation of GFP-PipB2 and LAMP-1."
FT /evidence="ECO:0000269|PubMed:15987736"
FT MUTAGEN 343
FT /note="N->A: Increases LAMP-1 redistribution. No effect on
FT peripheral accumulation of GFP-PipB2."
FT /evidence="ECO:0000269|PubMed:15987736"
FT MUTAGEN 344
FT /note="E->A: Decreases LAMP-1 redistribution. No effect on
FT peripheral accumulation of GFP-PipB2."
FT /evidence="ECO:0000269|PubMed:15987736"
FT MUTAGEN 345
FT /note="F->A: Prevents LE/Lys redistribution. Does not
FT affect the peripheral accumulation of GFP-PipB2."
FT /evidence="ECO:0000269|PubMed:15987736"
FT MUTAGEN 346
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:15987736"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:2LEZ"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:2LEZ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2LEZ"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:2LEZ"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2LEZ"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:2LEZ"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2LEZ"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2LEZ"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2LEZ"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:2LEZ"
SQ SEQUENCE 350 AA; 37274 MW; 701D5EFBA7EB11EF CRC64;
MERSLDSLAG MAKSAFGAGT SAAMRQATSP KTILEYIINF FTCGGIRRRN ETQYQELIET
MAETLKSTMP DRGAPLPENI ILDDMDGCRV EFNLPGENNE AGQVIVRVSK GDHSETREIP
LASFEKICRA LLFRCEFSLP QDSVILTAQG GMNLKGAVLT GANLTSENLC DADLSGANLE
GAVLFMADCE GANFKGANLS GTSLGDSNFK NACLEDSIMC GATLDHANLT GANLQHASLL
GCSMIECNCS GANMDHTNLS GATLIRADMS GATLQGATIM AAIMEGAVLT RANLRKASFI
STNLDGADLA EANLNNTCFK DCTLTDLRTE DATMSTSTQT LFNEFYSENI
