ID B1HPM4_LYSSC Unreviewed; 267 AA.
AC B1HPM4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=RNA-binding protein KhpB {ECO:0000256|HAMAP-Rule:MF_00867};
DE AltName: Full=RNA-binding protein EloR {ECO:0000256|HAMAP-Rule:MF_00867};
GN Name=khpB {ECO:0000256|HAMAP-Rule:MF_00867};
GN Synonyms=eloR {ECO:0000256|HAMAP-Rule:MF_00867};
GN OrderedLocusNames=Bsph_4782 {ECO:0000313|EMBL:ACA42226.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA42226.1, ECO:0000313|Proteomes:UP000002164};
RN [1] {ECO:0000313|EMBL:ACA42226.1, ECO:0000313|Proteomes:UP000002164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA42226.1,
RC ECO:0000313|Proteomes:UP000002164};
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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:0000256|HAMAP-Rule:MF_00867}.
CC -!- SUBUNIT: Forms a complex with KhpA. {ECO:0000256|HAMAP-Rule:MF_00867}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00867}.
CC -!- DOMAIN: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH
CC and R3H). {ECO:0000256|HAMAP-Rule:MF_00867}.
CC -!- SIMILARITY: Belongs to the KhpB RNA-binding protein family.
CC {ECO:0000256|HAMAP-Rule:MF_00867}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00867}.
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DR EMBL; CP000817; ACA42226.1; -; Genomic_DNA.
DR RefSeq; WP_012296224.1; NC_010382.1.
DR AlphaFoldDB; B1HPM4; -.
DR EnsemblBacteria; ACA42226; ACA42226; Bsph_4782.
DR KEGG; lsp:Bsph_4782; -.
DR HOGENOM; CLU_042512_0_0_9; -.
DR Proteomes; UP000002164; 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 CDD; cd02414; KH-II_Jag; 1.
DR CDD; cd02644; R3H_jag; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.30.30.80; probable RNA-binding protein from clostridium symbiosum atcc 14940; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR HAMAP; MF_00867; KhpB; 1.
DR InterPro; IPR038008; Jag_KH.
DR InterPro; IPR038247; Jag_N_dom_sf.
DR InterPro; IPR004087; KH_dom.
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 NCBIfam; NF041568; Jag_EloR; 1.
DR PANTHER; PTHR35800; PROTEIN JAG; 1.
DR PANTHER; PTHR35800:SF1; RNA-BINDING PROTEIN KHPB; 1.
DR Pfam; PF14804; Jag_N; 1.
DR Pfam; PF13083; KhpA-B_KH; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM01245; Jag_N; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00867};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00867};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00867};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00867};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00867}.
FT DOMAIN 199..265
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
SQ SEQUENCE 267 AA; 30244 MW; 8BA91297FBCF3004 CRC64;
MKQLTQIGAT TQEAISLALQ KLGKTREQVD VEVLQEGKKG FLGFGARSAE VRVTVKEVQI
PVIESEKAES QITTQLDKQL AVDDVETISS QVSDQPNEIE AVQKVVNEQN EEEDSANPIE
DAKTYLVTIA EQLDIHDLDI STTREGKYVY FQLKSEKAAL LIGKRGQTLN SLQQLTQLVL
NKSAKQFLMV KLDVENYRER RQEALELLAD RMADKALRSN QRVAFEPMPS YERKIIHNQL
ANRLDLETYS EGSEPNRYLV IEPVKNK
//
