ID   HRCQB_PSESH             Reviewed;         128 AA.
AC   O85094;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Type III secretion protein HrcQb;
GN   Name=hrcQb; Synonyms=hrcQ2, hrpU;
OS   Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS   phaseolicola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NPS 3121;
RA   Frederick R.D., Panopoulos N.J.;
RT   "The hrpD locus of Pseudomonas syringae pv. phaseolicola encodes the five
RT   most broadly conserved proteins in the signal peptide independent (type
RT   III) protein export system common to plant and animal pathogenic
RT   bacteria.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NPS 3121;
RX   AGRICOLA=IND43617657; DOI=10.1111/j.1364-3703.2004.00212.x;
RA   Gropp S.J., Guttman D.S.;
RT   "The PCR amplification and characterization of entire Pseudomonas syringae
RT   hrp/hrc clusters.";
RL   Mol. Plant Pathol. 5:137-140(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 50-128.
RX   PubMed=11679746; DOI=10.1107/s0907444901012999;
RA   Fadouloglou V.E., Tampakaki A.P., Panopoulos N.J., Kokkinidis M.;
RT   "Structural studies of the Hrp secretion system: expression, purification,
RT   crystallization and preliminary X-ray analysis of the C-terminal domain of
RT   the HrcQB protein from Pseudomonas syringae pv. phaseolicola.";
RL   Acta Crystallogr. D 57:1689-1691(2001).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 50-128.
RX   PubMed=14694203; DOI=10.1073/pnas.0304579101;
RA   Fadouloglou V.E., Tampakaki A.P., Glykos N.M., Bastaki M.N., Hadden J.M.,
RA   Phillips S.E., Panopoulos N.J., Kokkinidis M.;
RT   "Structure of HrcQb-C, a conserved component of the bacterial type III
RT   secretion systems.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:70-75(2004).
CC   -!- FUNCTION: Component of the type III secretion system, which is required
CC       for effector protein delivery, parasitism, and pathogenicity. Probably
CC       participates in the formation of a C-ring-like assembly along with
CC       HrcQa.
CC   -!- SUBUNIT: Homotetramer. The four monomers assemble into two tightly
CC       bound homodimers. Interacts with HrcQa.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Or loosely associated with a
CC       membrane component, probably HrcQa.
CC   -!- DOMAIN: The HrcQb-C domain interacts with the HrcQa C-terminal domain.
CC   -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family. {ECO:0000305}.
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DR   EMBL; AF043444; AAC25068.1; -; Genomic_DNA.
DR   EMBL; AY530203; AAS20443.1; -; Genomic_DNA.
DR   RefSeq; WP_004666088.1; NZ_RBUR01000293.1.
DR   PDB; 1O9Y; X-ray; 2.29 A; A/B/C/D=50-128.
DR   PDBsum; 1O9Y; -.
DR   AlphaFoldDB; O85094; -.
DR   SMR; O85094; -.
DR   OMA; CHGEQVV; -.
DR   EvolutionaryTrace; O85094; -.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   Gene3D; 2.30.330.10; -; 1.
DR   InterPro; IPR001543; FliN-like_C.
DR   InterPro; IPR001172; FliN_T3SS_HrcQb.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   Pfam; PF01052; FliMN_C; 1.
DR   PRINTS; PR00956; FLGMOTORFLIN.
DR   SUPFAM; SSF101801; SSF101801; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Virulence.
FT   CHAIN           1..128
FT                   /note="Type III secretion protein HrcQb"
FT                   /id="PRO_0000184134"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..128
FT                   /note="HrcQb-C"
FT   REGION          78..81
FT                   /note="Dimer-dimer interface"
FT   COMPBIAS        1..17
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            87
FT                   /note="Dimer-dimer interface"
FT   SITE            112
FT                   /note="Dimer-dimer interface"
FT   SITE            114
FT                   /note="Dimer-dimer interface"
FT   SITE            120
FT                   /note="Dimer-dimer interface"
FT   STRAND          60..73
FT                   /evidence="ECO:0007829|PDB:1O9Y"
FT   HELIX           74..78
FT                   /evidence="ECO:0007829|PDB:1O9Y"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:1O9Y"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:1O9Y"
FT   STRAND          103..113
FT                   /evidence="ECO:0007829|PDB:1O9Y"
FT   STRAND          116..124
FT                   /evidence="ECO:0007829|PDB:1O9Y"
SQ   SEQUENCE   128 AA;  14077 MW;  4EB7C417E435271B CRC64;
     MSTEDLYQED VEMLDDYEDP STEQHWSEED GEPSGYATAE PDDHAAQEEQ DEPPALDSLA
     LDLTLRCGEL RLTLAELRRL DAGTILEVTG ISPGHATLCH GEQVVAEGEL VDVEGRLGLQ
     ITRLVTRS