KHPA_STRR6
ID KHPA_STRR6 Reviewed; 79 AA.
AC Q8DQG4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=RNA-binding protein KhpA {ECO:0000255|HAMAP-Rule:MF_00088};
DE AltName: Full=KH-domain protein A {ECO:0000255|HAMAP-Rule:MF_00088, ECO:0000303|PubMed:30842445};
GN Name=khpA {ECO:0000255|HAMAP-Rule:MF_00088, ECO:0000303|PubMed:30842445};
GN OrderedLocusNames=spr0683;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, INTERACTION WITH KHPB (ELOR), SUBUNIT, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 50-ARG-LYS-51; ARG-53; ARG-59;
RP THR-60 AND ILE-61.
RC STRAIN=R6 / R704;
RX PubMed=30842445; DOI=10.1038/s41598-018-38386-6;
RA Winther A.R., Kjos M., Stamsaas G.A., Haavarstein L.S., Straume D.;
RT "Prevention of EloR/KhpA heterodimerization by introduction of site-
RT specific amino acid substitutions renders the essential elongasome protein
RT PBP2b redundant in Streptococcus pneumoniae.";
RL Sci. Rep. 9:3681-3681(2019).
CC -!- FUNCTION: A probable RNA chaperone. Forms a complex with KhpB which
CC binds to cellular RNA and controls its expression. Plays a role in
CC peptidoglycan (PG) homeostasis and cell length regulation.
CC {ECO:0000255|HAMAP-Rule:MF_00088, ECO:0000269|PubMed:30842445}.
CC -!- FUNCTION: The KhpA-KhpB complex stimulates or controls elongasome-
CC mediated lateral cell wall biosynthesis. It is not clear what is the
CC function of the KhpA homooligomer in vivo.
CC {ECO:0000269|PubMed:30842445}.
CC -!- SUBUNIT: Self-associates, makes at least homodimers. Interacts with
CC KhpB (also called EloR) via the KH domain of KhpB. The complex with
CC KhpB is critical for regulating elongasome activity and for KhpA
CC localization at midcell. {ECO:0000269|PubMed:30842445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00088,
CC ECO:0000305|PubMed:30842445}. Note=Some protein localizes to the
CC division zone with FtsZ throughout the cell cycle, the rest remains in
CC the cytoplasm. {ECO:0000269|PubMed:30842445}.
CC -!- DISRUPTION PHENOTYPE: Cells grow more slowly, are rounder with less
CC elongation, form short chains. {ECO:0000269|PubMed:30842445}.
CC -!- SIMILARITY: Belongs to the KhpA RNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00088}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007317; AAK99487.1; -; Genomic_DNA.
DR PIR; A95090; A95090.
DR PIR; C97957; C97957.
DR RefSeq; NP_358277.1; NC_003098.1.
DR RefSeq; WP_000379621.1; NC_003098.1.
DR AlphaFoldDB; Q8DQG4; -.
DR STRING; 171101.spr0683; -.
DR EnsemblBacteria; AAK99487; AAK99487; spr0683.
DR GeneID; 60234071; -.
DR GeneID; 66805920; -.
DR KEGG; spr:spr0683; -.
DR PATRIC; fig|171101.6.peg.756; -.
DR eggNOG; COG1837; Bacteria.
DR HOGENOM; CLU_132074_1_2_9; -.
DR OMA; HETDEYM; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_00088; KhpA; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR020627; KhpA.
DR PANTHER; PTHR34654; PTHR34654; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW Reference proteome; RNA-binding.
FT CHAIN 1..79
FT /note="RNA-binding protein KhpA"
FT /id="PRO_0000454540"
FT DOMAIN 32..79
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00088"
FT MUTAGEN 50..51
FT /note="RK->DD: Still self-interacts, still interacts with
FT KhpB, pbp2b can be deleted."
FT /evidence="ECO:0000269|PubMed:30842445"
FT MUTAGEN 53
FT /note="R->K: Still self-interacts."
FT /evidence="ECO:0000269|PubMed:30842445"
FT MUTAGEN 59
FT /note="R->K: Still self-interacts."
FT /evidence="ECO:0000269|PubMed:30842445"
FT MUTAGEN 60
FT /note="T->Q: Still self-interacts."
FT /evidence="ECO:0000269|PubMed:30842445"
FT MUTAGEN 61
FT /note="I->F: Loss of self-interaction, still interacts with
FT KhpB, cells grow at wild-type rate, pbp2b cannot be
FT deleted, some KhpA found at midcell."
FT /evidence="ECO:0000269|PubMed:30842445"
FT MUTAGEN 61
FT /note="I->Y: Loss of self-interaction, no longer interacts
FT with KhpB, cells are rounder with less elongation, form
FT short chains, pbp2b can be deleted, no KhpA found at
FT midcell."
FT /evidence="ECO:0000269|PubMed:30842445"
SQ SEQUENCE 79 AA; 8994 MW; B1903EBCA8CC9134 CRC64;
MDTIENLIIA IVKPLISQPD ALTIKIEDTP EFLEYHLNLD QSDVGRVIGR KGRTISAIRT
IVYSVPTEYK KVRIVIDEK
