KHPA_STRPN
ID KHPA_STRPN Reviewed; 79 AA.
AC A0A0H2UPF7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
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:28941257};
GN Name=khpA {ECO:0000255|HAMAP-Rule:MF_00088, ECO:0000303|PubMed:28941257};
GN OrderedLocusNames=SP_0776;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=28941257; DOI=10.1111/mmi.13847;
RA Zheng J.J., Perez A.J., Tsui H.T., Massidda O., Winkler M.E.;
RT "Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses
RT the requirement for PBP2b by overproduction of FtsA in Streptococcus
RT pneumoniae D39.";
RL Mol. Microbiol. 106:793-814(2017).
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:28941257}.
CC -!- FUNCTION: Probably plays a role in PG homeostasis and regulating
CC peripheral PG synthesis. {ECO:0000305|PubMed:28941257}.
CC -!- SUBUNIT: Forms a complex with KhpB. {ECO:0000255|HAMAP-Rule:MF_00088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00088}.
CC -!- DISRUPTION PHENOTYPE: Grows slowly and is smaller than wild-type;
CC estimated to be about 50% of the volume of wild-type cells.
CC {ECO:0000269|PubMed:28941257}.
CC -!- SIMILARITY: Belongs to the KhpA RNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00088}.
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DR EMBL; AE005672; AAK74914.1; -; Genomic_DNA.
DR RefSeq; WP_000379621.1; NZ_AKVY01000001.1.
DR STRING; 170187.SP_0776; -.
DR EnsemblBacteria; AAK74914; AAK74914; SP_0776.
DR GeneID; 60234071; -.
DR GeneID; 66805920; -.
DR KEGG; spn:SP_0776; -.
DR eggNOG; COG1837; Bacteria.
DR OMA; HETDEYM; -.
DR PhylomeDB; A0A0H2UPF7; -.
DR BioCyc; SPNE170187:G1FZB-791-MON; -.
DR Proteomes; UP000000585; 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 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Chaperone; Cytoplasm;
KW RNA-binding.
FT CHAIN 1..79
FT /note="RNA-binding protein KhpA"
FT /id="PRO_0000454539"
FT DOMAIN 32..79
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00088"
SQ SEQUENCE 79 AA; 8994 MW; B1903EBCA8CC9134 CRC64;
MDTIENLIIA IVKPLISQPD ALTIKIEDTP EFLEYHLNLD QSDVGRVIGR KGRTISAIRT
IVYSVPTEYK KVRIVIDEK