ID B2KE66_ELUMP Unreviewed; 470 AA.
AC B2KE66;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=Emin_1262 {ECO:0000313|EMBL:ACC98812.1};
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98812.1, ECO:0000313|Proteomes:UP000001029};
RN [1] {ECO:0000313|EMBL:ACC98812.1, ECO:0000313|Proteomes:UP000001029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC98812.1,
RC ECO:0000313|Proteomes:UP000001029};
RX PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC98812.1; -; Genomic_DNA.
DR RefSeq; WP_012415427.1; NC_010644.1.
DR AlphaFoldDB; B2KE66; -.
DR STRING; 445932.Emin_1262; -.
DR KEGG; emi:Emin_1262; -.
DR HOGENOM; CLU_581067_0_0_0; -.
DR OrthoDB; 9794483at2; -.
DR Proteomes; UP000001029; 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; 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; SM00393; R3H; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00867};
KW Reference proteome {ECO:0000313|Proteomes:UP000001029};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00867}.
FT DOMAIN 241..307
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 73..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 74..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 52282 MW; 322027AE587E54FD CRC64;
MPKKIKIEAK DVDTAINNGL KEIGLRRDQV EVSVLARPTK GFWGIGAKPA VVEIRQKRWG
GNLDAQIYMD VPKKRGGFNK RNNNRKKEDD FKRDPEGSRV NKKTSNNRGG KKNFGRKDKI
RKQRPVSTEP KAPKENEAQL LPSQAIQNAV IPENLKAPMA EGKEMLFKML EQMGIKTENL
NVWWDSAQQR ILLTFDCDHP AIVIGKEGKT LEAIQYLLTL SLSRHFSTPI SVVADTQNYW
RKSEDKLYAE IDRAVNAIKR GANVYRLKPM PAQMRRFIHR ALETNEFVET ASEGEGKWRK
VVIKERVSTI EPKVVTEAEK AADAAARTPE KCASEQLDKE VDAAQENLDE QIKAERAAEK
AARAQAQAAT PVLDAADISA ATQSPAGVEE EASSCSENVE INGEQVSICT VEVEKEEVVL
KEAPSSQDQV EGTSCGMLEV ELKPGGDVTE EVKEAEAEQT KEENKETPAP
//
