KHPB_STRR6
ID KHPB_STRR6 Reviewed; 328 AA.
AC Q8CY87;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=RNA-binding protein KhpB {ECO:0000255|HAMAP-Rule:MF_00867};
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:0000305};
DE AltName: Full=RNA-binding protein EloR {ECO:0000255|HAMAP-Rule:MF_00867};
DE AltName: Full=RNA-binding protein Jag {ECO:0000303|PubMed:27776484};
GN Name=khpB {ECO:0000255|HAMAP-Rule:MF_00867};
GN Synonyms=eloR {ECO:0000255|HAMAP-Rule:MF_00867,
GN ECO:0000303|PubMed:28710862}, jag {ECO:0000303|PubMed:27776484};
GN OrderedLocusNames=spr1851;
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, DOMAIN, PHOSPHORYLATION AT
RP THR-89, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-89.
RC STRAIN=Rx1;
RX PubMed=27776484; DOI=10.1186/s12866-016-0865-6;
RA Ulrych A., Holeckova N., Goldova J., Doubravova L., Benada O.,
RA Kofronova O., Halada P., Branny P.;
RT "Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant
RT and identification of a novel PhpP substrate, putative RNA binding protein
RT Jag.";
RL BMC Microbiol. 16:247-247(2016).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF THR-89; 228-TYR-HIS-229 AND 297-ARG--HIS-301.
RC STRAIN=R6 / R704;
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 [4]
RP FUNCTION, INTERACTION WITH KHPA, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LEU-239.
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).
RN [5]
RP INTERACTION WITH MLTG; RODZ AND YIDC2, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=R6 / R704;
RX PubMed=33558392; DOI=10.1128/jb.00691-20;
RA Winther A.R., Kjos M., Herigstad M.L., Haavarstein L.S., Straume D.;
RT "EloR interacts with the lytic transglycosylase MltG at midcell in
RT Streptococcus pneumoniae R6.";
RL J. Bacteriol. 0:0-0(2021).
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 stimulates or controls
CC elongasome-mediated lateral cell wall biosynthesis (PubMed:30842445).
CC RNA-bonding protein; overexpression leads to cell elongation,
CC suggesting it plays a role in cell division and maintenance of cell
CC shape (PubMed:27776484). In cell elongation the phosphorylated form
CC activates cell elongation while the non-phosphorylated form is less
CC active or inactive (Probable). Probably plays a role in regulation of
CC other RNAs (By similarity). {ECO:0000250|UniProtKB:A0A0H2ZPS7,
CC ECO:0000269|PubMed:27776484, ECO:0000269|PubMed:30842445,
CC ECO:0000305|PubMed:28710862}.
CC -!- SUBUNIT: Interacts with StkP which phosphorylates it (PubMed:27776484,
CC PubMed:28710862). Interacts with KhpA via the KH domain of this protein
CC (PubMed:30842445). Interacts with MreC in the elongasome
CC (PubMed:28710862). Interacts with MltG, RodZ and YidC2, interacts with
CC MltG's N-terminus (PubMed:33558392). {ECO:0000269|PubMed:27776484,
CC ECO:0000269|PubMed:28710862, ECO:0000269|PubMed:30842445,
CC ECO:0000269|PubMed:33558392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00867,
CC ECO:0000305|PubMed:28710862}. Note=Localizes to midcell in the septal
CC area; some protein remains in the cytoplasm.
CC {ECO:0000269|PubMed:28710862, ECO:0000269|PubMed:33558392}.
CC -!- DOMAIN: Has an N-terminal Jag-N, a linker with a phosphorylated Thr,
CC and 2 RNA-binding domains (KH and R3H) (Probable). A phosphomimetic
CC mutation and mutations that prevent nucleic acid binding are not
CC tolerated in strain R6 (PubMed:28710862). The KH domain of this protein
CC interacts with KhpA (PubMed:30842445). The Jag-N domain is responsible
CC for targeting to the midcell (PubMed:33558392).
CC {ECO:0000269|PubMed:28710862, ECO:0000269|PubMed:30842445,
CC ECO:0000269|PubMed:33558392, ECO:0000305|PubMed:27776484,
CC ECO:0000305|PubMed:28710862}.
CC -!- PTM: Phosphorylated on Thr-89 by StkP; there is another phosphorylated
CC Thr residue in the protein, which is more strongly phosphorylated in
CC strain R6 than in Rx1 (PubMed:27776484, PubMed:28710862).
CC Dephosphorylated by PhpP (PubMed:27776484). Phosphorylation is
CC increased in an R6 strain with a C-terminal MreC deletion
CC (PubMed:28710862). {ECO:0000269|PubMed:27776484,
CC ECO:0000269|PubMed:28710862}.
CC -!- DISRUPTION PHENOTYPE: Grows more slowly with a longer lag phase and
CC decreased final density compared to wild-type. Cells are significantly
CC smaller (PubMed:27776484, PubMed:28710862). Suppresses deletions of
CC PBP2b (penA). Double penA-khpB or rodA-khpB deletions partially
CC alleviate the slow growth phenotype of the single deletion
CC (PubMed:28710862). KhpA is no longer targeted to midcell
CC (PubMed:30842445). {ECO:0000269|PubMed:27776484,
CC ECO:0000269|PubMed:28710862, ECO:0000269|PubMed:30842445}.
CC -!- MISCELLANEOUS: Strain Rx1 is unencapsulated.
CC {ECO:0000305|PubMed:27776484}.
CC -!- SIMILARITY: Belongs to the KhpB RNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00867}.
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; AAL00654.1; -; Genomic_DNA.
DR PIR; A99703; A99703.
DR PIR; H95238; H95238.
DR RefSeq; NP_359443.1; NC_003098.1.
DR RefSeq; WP_000260012.1; NC_003098.1.
DR AlphaFoldDB; Q8CY87; -.
DR STRING; 171101.spr1851; -.
DR EnsemblBacteria; AAL00654; AAL00654; spr1851.
DR GeneID; 60233791; -.
DR KEGG; spr:spr1851; -.
DR PATRIC; fig|171101.6.peg.1997; -.
DR eggNOG; COG1847; Bacteria.
DR HOGENOM; CLU_042512_0_0_9; -.
DR OMA; INQKHAP; -.
DR Proteomes; UP000000586; 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; Reference proteome; RNA-binding.
FT CHAIN 1..328
FT /note="RNA-binding protein KhpB"
FT /id="PRO_0000454544"
FT DOMAIN 181..258
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00867,
FT ECO:0000305|PubMed:27776484, ECO:0000305|PubMed:28710862"
FT DOMAIN 263..328
FT /note="R3H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00867,
FT ECO:0000305|PubMed:27776484, ECO:0000305|PubMed:28710862"
FT REGION 3..53
FT /note="Jag_N domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00867,
FT ECO:0000305|PubMed:27776484, ECO:0000305|PubMed:28710862"
FT REGION 54..180
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:27776484,
FT ECO:0000305|PubMed:28710862"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27776484"
FT MUTAGEN 89
FT /note="T->A: Nearly complete loss of phosphothreonine
FT (strain Rx1), loss of 1 phosphothreonine (in strain R6). In
FT R6 cells are significantly smaller."
FT /evidence="ECO:0000269|PubMed:27776484,
FT ECO:0000269|PubMed:28710862"
FT MUTAGEN 89
FT /note="T->E: Can only be found in strain R6 cells when mreC
FT or rodZ acquire suppressor mutations; cells are
FT significantly smaller."
FT /evidence="ECO:0000269|PubMed:28710862"
FT MUTAGEN 228..229
FT /note="YH->DD: Can only be found in strain R6 cells when
FT rodZ acquires suppressor mutations; cells are significantly
FT smaller."
FT /evidence="ECO:0000269|PubMed:28710862"
FT MUTAGEN 239
FT /note="L->Y: Loss of interaction with KhpA, pbp2b can be
FT deleted, KphA not found at midcell."
FT /evidence="ECO:0000269|PubMed:30842445"
FT MUTAGEN 297..301
FT /note="RKIIH->KKIIY: Can only be found in strain R6 cells
FT when mreC acquires suppressor mutations; cells are
FT significantly smaller."
FT /evidence="ECO:0000269|PubMed:28710862"
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
