ID   PIPB2_SALCH             Reviewed;         350 AA.
AC   Q57KZ6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Secreted effector protein PipB2;
DE   AltName: Full=Type III effector PipB2;
GN   Name=pipB2; OrderedLocusNames=SCH_2710;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the host kinesin light chain (KLC), a subunit
CC       of the kinesin-1 motor complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host membrane
CC       {ECO:0000250}. Note=Secreted via the type III secretion system 2 (SPI-2
CC       TTSS), and delivered into the host cell. {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AE017220; AAX66616.1; -; Genomic_DNA.
DR   RefSeq; WP_001540738.1; NC_006905.1.
DR   AlphaFoldDB; Q57KZ6; -.
DR   BMRB; Q57KZ6; -.
DR   SMR; Q57KZ6; -.
DR   EnsemblBacteria; AAX66616; AAX66616; SCH_2710.
DR   KEGG; sec:SCH_2710; -.
DR   HOGENOM; CLU_067808_0_0_6; -.
DR   OMA; ADCDGAN; -.
DR   Proteomes; UP000000538; 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   3: Inferred from homology;
KW   Host membrane; Membrane; Repeat; Secreted; Virulence.
FT   CHAIN           1..350
FT                   /note="Secreted effector protein PipB2"
FT                   /id="PRO_0000278296"
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"
SQ   SEQUENCE   350 AA;  37338 MW;  289E6CF0740B4864 CRC64;
     MQRSLDSLAG MATSAFGAGT SAAMRQATSP KTILEYIINF FTCGGIRRRN ETQYQELIET
     MAETLKSTMP DRGAPLPENI ILDDMDGCRV EFNLPGENNE AGQVIVRVSK GDHSETREIP
     LVSFEKICRA LLFRCEFSLP QDSVILTAQG GMNLKGAVLT GANLTAENLC DADLSGANLE
     GAVLFMADCE GANFKGANLS GTSLGDSNFK NACLEDSIMC GATLDHANLT GANLQHASLL
     GCSMIECNCS GANMDHTNLS GATLIRADMS GATLQGATIM AAIMEDAVLT RANLRKASFI
     STNLDGADLA EANLNNTCFK DCTLTHLRTE DATMSTSTQT LFNEFYSENI