ID K6P0Z0_9FIRM Unreviewed; 231 AA.
AC K6P0Z0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=ThesuDRAFT_00474 {ECO:0000313|EMBL:EKP94770.1};
OS Thermaerobacter subterraneus DSM 13965.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=867903 {ECO:0000313|EMBL:EKP94770.1, ECO:0000313|Proteomes:UP000005710};
RN [1] {ECO:0000313|EMBL:EKP94770.1, ECO:0000313|Proteomes:UP000005710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13965 {ECO:0000313|EMBL:EKP94770.1,
RC ECO:0000313|Proteomes:UP000005710};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R.,
RA Wahrenburg C., Brambilla E., Klenk H.-P., Eisen J.A.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EKP94770.1, ECO:0000313|Proteomes:UP000005710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13965 {ECO:0000313|EMBL:EKP94770.1,
RC ECO:0000313|Proteomes:UP000005710};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.;
RT "Improved high-quality draft of Thermaerobacter subterraneus C21, DSM
RT 13965.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKP94770.1}.
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; AENY02000002; EKP94770.1; -; Genomic_DNA.
DR RefSeq; WP_006902755.1; NZ_JH976535.1.
DR AlphaFoldDB; K6P0Z0; -.
DR STRING; 867903.ThesuDRAFT_00474; -.
DR eggNOG; COG1847; Bacteria.
DR HOGENOM; CLU_042512_0_1_9; -.
DR OrthoDB; 9794483at2; -.
DR Proteomes; UP000005710; Unassembled WGS sequence.
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 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 152..218
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 16..66
FT /note="Jag_N domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00867"
SQ SEQUENCE 231 AA; 25327 MW; D237CFF52AEE0DB4 CRC64;
MSAAFREVLG AGPWIETRGR TVEEALEAAA RRLGVGREAL EARVVAEPSR GFLGLVGQRD
AVVQARVRPT KARFAAAFLE ELARAAGLAV QVAVEEGPDR ILARMEGGPE LGALIGRRGV
ALEALQYLLN VAAARVSEEQ RRVVLDVAGY RERRRQSLER LALRMAERAR RTRRPVTLEP
MPAAERRVVH LALQNHPEVR TESTGTEPYR RVVIVPRRPG RGGVSTGTGR P
//