KHPA_STRP2
ID KHPA_STRP2 Reviewed; 79 AA.
AC A0A0H2ZMB4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=RNA-binding protein KhpA {ECO:0000255|HAMAP-Rule:MF_00088, ECO:0000303|PubMed:28941257};
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=SPD_0675;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2]
RP FUNCTION, INTERACTION WITH KHPB, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, RNA-BINDING, AND MUTAGENESIS OF 49-GLY--GLY-52; GLY-49;
RP 50-ARG-LYS-51; GLY-52 AND 72-VAL--LYS-79.
RC STRAIN=D39 / NCTC 7466;
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 presumably binds to about 170 cellular RNAs (mRNA, tRNA intergenic RNA
CC and sRNAs); the proteins alone each bind the same set of RNAs. A
CC mutation in this gene suppresses the requirement for PBP2b (penA, a
CC transpeptidase) in peripheral peptidogylcan (PG) synthesis
CC (PubMed:28941257). Probably plays a role in PG homeostasis and
CC regulating peripheral PG synthesis (PubMed:28941257).
CC {ECO:0000269|PubMed:28941257, ECO:0000305|PubMed:28941257}.
CC -!- SUBUNIT: Forms a complex with KhpB (By similarity) (PubMed:28941257).
CC KhpA and KhpB colocalize throughout the cell cycle, with some increase
CC at midcell in dividing cells (PubMed:28941257). {ECO:0000255|HAMAP-
CC Rule:MF_00088, ECO:0000269|PubMed:28941257}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00088,
CC ECO:0000305|PubMed:28941257}. Note=Some protein localizes to midcell in
CC the septal area, the rest remains in the cytoplasm.
CC {ECO:0000269|PubMed:28941257}.
CC -!- DISRUPTION PHENOTYPE: Suppresses a pbp2b (penA) deletion, grows slowly
CC and is smaller than wild-type; about 50% of the volume of wild-type
CC cells. Increased accumulation of FtsA and FtsZ proteins. Significant
CC up-regulation of genes of the WalRK regulon. Also partially suppresses
CC deletions in other genes involved in peripheral PG synthesis; gpsB,
CC mreCD, rodA and rodZ but not cozE or mltG. Slight increase in net
CC phosphorylation (by StpK/PhpP) of DivIA, slight decrease in
CC phosphorylation of MapZ/StpK. Double khpA-khpB deletions have the same
CC phenotypes. {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; CP000410; ABJ53899.1; -; Genomic_DNA.
DR RefSeq; WP_000379621.1; NC_008533.2.
DR STRING; 373153.SPD_0675; -.
DR EnsemblBacteria; ABJ53899; ABJ53899; SPD_0675.
DR GeneID; 60234071; -.
DR GeneID; 66805920; -.
DR KEGG; spd:SPD_0675; -.
DR eggNOG; COG1837; Bacteria.
DR HOGENOM; CLU_132074_1_2_9; -.
DR OMA; HETDEYM; -.
DR OrthoDB; 1940160at2; -.
DR BioCyc; SPNE373153:G1G6V-744-MON; -.
DR Proteomes; UP000001452; 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; Chaperone; Cytoplasm;
KW RNA-binding.
FT CHAIN 1..79
FT /note="RNA-binding protein KhpA"
FT /id="PRO_0000454538"
FT DOMAIN 32..79
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00088"
FT MUTAGEN 49..52
FT /note="GRKG->ARKA: Decreased amount of protein, slow
FT growth."
FT /evidence="ECO:0000269|PubMed:28941257"
FT MUTAGEN 49
FT /note="G->A: 50% protein, intermediate growth rate."
FT /evidence="ECO:0000269|PubMed:28941257"
FT MUTAGEN 50..51
FT /note="RK->DD: Decreased amount of protein, slow growth."
FT /evidence="ECO:0000269|PubMed:28941257"
FT MUTAGEN 52
FT /note="G->A: Nearly wild-type protein level, wild-type
FT growth rate."
FT /evidence="ECO:0000269|PubMed:28941257"
FT MUTAGEN 72..79
FT /note="Missing: Suppresses a pbp2b (penA) deletion."
FT /evidence="ECO:0000269|PubMed:28941257"
SQ SEQUENCE 79 AA; 8994 MW; B1903EBCA8CC9134 CRC64;
MDTIENLIIA IVKPLISQPD ALTIKIEDTP EFLEYHLNLD QSDVGRVIGR KGRTISAIRT
IVYSVPTEYK KVRIVIDEK
