KHPB_STRP2
ID KHPB_STRP2 Reviewed; 328 AA.
AC A0A0H2ZPS7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=RNA-binding protein KhpB {ECO:0000255|HAMAP-Rule:MF_00867, ECO:0000303|PubMed:28941257};
DE AltName: Full=Elongasome regulating protein {ECO:0000303|PubMed:28710862};
DE Short=EloR {ECO:0000303|PubMed:28710862};
DE AltName: Full=KH-domain protein B {ECO:0000303|PubMed:28941257};
DE AltName: Full=RNA-binding protein EloR {ECO:0000255|HAMAP-Rule:MF_00867};
DE AltName: Full=RNA-binding protein Jag {ECO:0000305};
GN Name=kphB {ECO:0000255|HAMAP-Rule:MF_00867, ECO:0000303|PubMed:28941257};
GN Synonyms=eloR {ECO:0000255|HAMAP-Rule:MF_00867}, jag {ECO:0000305};
GN OrderedLocusNames=SPD_1849;
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 PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=28710862; DOI=10.1111/mmi.13748;
RA Stamsaas G.A., Straume D., Ruud Winther A., Kjos M., Frantzen C.A.,
RA Haavarstein L.S.;
RT "Identification of EloR (Spr1851) as a regulator of cell elongation in
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 105:954-967(2017).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH KHPA,
RP SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, RNA-BINDING,
RP AND MUTAGENESIS OF THR-89.
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 KhpA 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_00867}.
CC -!- FUNCTION: Forms a complex with KhpA which presumably binds to about 170
CC cellular RNAs (mRNA, tRNA intergenic RNA and sRNAs); the proteins alone
CC each bind the same set of RNAs. Suppresses the requirement for PBP2b
CC (penA, a transpeptidase) in peripheral peptidogylcan (PG) synthesis
CC (PubMed:28941257). May function as a pleiotropic RNA chaperone
CC controlling pneumococcal cell division, including PG homeostasis and
CC regulating peripheral PG synthesis by the elongasome (Probable).
CC {ECO:0000269|PubMed:28941257, ECO:0000305|PubMed:28941257}.
CC -!- SUBUNIT: Interacts with KhpA; the 2 proteins colocalize throughout the
CC cell cycle, with some increase at midcell in dividing cells
CC (PubMed:28941257). Interacts with StkP which phosphorylates it,
CC interacts with MltG, MreC, RodZ and YidC2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8CY87, ECO:0000269|PubMed:28941257}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00867,
CC ECO:0000305|PubMed:28710862}. Note=Some protein localizes to midcell in
CC the septal area, the rest remains in the cytoplasm.
CC {ECO:0000269|PubMed:28710862}.
CC -!- DOMAIN: Has an N-terminal Jag-N domain, a linker with a phosphorylated
CC Thr, and 2 RNA-binding domains (KH and R3H).
CC {ECO:0000305|PubMed:28941257}.
CC -!- PTM: Phosphorylated on Thr-89 by StkP; there is another poorly
CC phosphorylated residue in the protein. Dephosphorylated by PhpP.
CC {ECO:0000250|UniProtKB:Q8CY87}.
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 protein. Significant up-
CC 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 mltG. Slight decrease in net
CC phosphorylation (by StpK/PhpP) of DivIA and MapZ/StpK. Double khpA-khpB
CC deletions have the same phenotypes. {ECO:0000269|PubMed:28941257}.
CC -!- SIMILARITY: Belongs to the KhpB RNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00867}.
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DR EMBL; CP000410; ABJ55280.1; -; Genomic_DNA.
DR RefSeq; WP_000260012.1; NC_008533.2.
DR STRING; 373153.SPD_1849; -.
DR EnsemblBacteria; ABJ55280; ABJ55280; SPD_1849.
DR GeneID; 60233791; -.
DR KEGG; spd:SPD_1849; -.
DR eggNOG; COG1847; Bacteria.
DR HOGENOM; CLU_042512_0_0_9; -.
DR OMA; INQKHAP; -.
DR OrthoDB; 1304273at2; -.
DR BioCyc; SPNE373153:G1G6V-1995-MON; -.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd02414; jag_KH; 1.
DR CDD; cd02644; R3H_jag; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.30.30.80; -; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR HAMAP; MF_00867; KhpB; 1.
DR InterPro; IPR038008; Jag_KH.
DR InterPro; IPR038247; Jag_N_dom_sf.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR039247; KhpB.
DR InterPro; IPR032782; KhpB_N.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034079; R3H_KhpB.
DR PANTHER; PTHR35800; PTHR35800; 1.
DR Pfam; PF14804; Jag_N; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM01245; Jag_N; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Chaperone; Cytoplasm;
KW Phosphoprotein; RNA-binding.
FT CHAIN 1..328
FT /note="RNA-binding protein KhpB"
FT /id="PRO_0000454543"
FT DOMAIN 181..258
FT /note="KH"
FT /evidence="ECO:0000305|PubMed:28941257"
FT DOMAIN 263..328
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382,
FT ECO:0000305|PubMed:28941257"
FT REGION 3..53
FT /note="Jag_N domain"
FT /evidence="ECO:0000305|PubMed:28941257"
FT REGION 54..180
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:28941257"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CY87"
FT MUTAGEN 89
FT /note="T->A,D,E: No visible effect on cell growth or
FT shape."
FT /evidence="ECO:0000269|PubMed:28941257"
SQ SEQUENCE 328 AA; 37110 MW; 162BBC1B10CDC109 CRC64;
MVVFTGSTVE EAIQKGLKEL DIPRMKAHIK VISREKKGFL GLFGKKPAQV DIEAISETTV
VKANQQVVKG VPKKINDLNE PVKTVSEETV DLGHVVDAIK KIEEEGQGIS DEVKAEILKH
ERHASTILEE TGHIEILNEL QIEEAMREEA GADDLETEQD QAESQELEDL GLKVETNFDI
EQVATEVMAY VQTIIDDMDV EATLSNDYNR RSINLQIDTN EPGRIIGYHG KVLKALQLLA
QNYLYNRYSR TFYVTINVND YVEHRAEVLQ TYAQKLATRV LEEGRSHKTD PMSNSERKII
HRIISRMDGV TSYSEGDEPN RYVVVDTE
