ID A0A416RED3_9FIRM Unreviewed; 341 AA.
AC A0A416RED3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DWX58_05510 {ECO:0000313|EMBL:RHR10837.1};
OS Pseudoflavonifractor sp. AF19-9AC.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=2292244 {ECO:0000313|EMBL:RHR10837.1, ECO:0000313|Proteomes:UP000285063};
RN [1] {ECO:0000313|EMBL:RHR10837.1, ECO:0000313|Proteomes:UP000285063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF19-9AC {ECO:0000313|EMBL:RHR10837.1,
RC ECO:0000313|Proteomes:UP000285063};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:RHR10837.1}.
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DR EMBL; QUGI01000002; RHR10837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416RED3; -.
DR Proteomes; UP000285063; 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; PS50084; KH_TYPE_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000285063};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00867}.
FT DOMAIN 272..338
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 114..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37582 MW; DFC9A70651C7DC07 CRC64;
MRKWIETTGR SEEDAIAAAL FQLGLERDDV SVEVMERAKS GFLGFGSNPA KVRVSYEEEN
GVPKPIKDPL EEDLFAAVKE APKAQPKPAP VVEQKAAPVS APVEETVLAA APVQEAPKEE
APVEEETILA AKPGWEAPKP RREARPRRER QEKPRHARNE LQEGDEVIIG AQEPRPAPAP
ILDPASPDDQ KAQQIVTFLT GLLERLEVEA VPQVLGGPET GYKVILQGTG LGAIIGRRGE
TLDAIQQLTN YAVNHGQSKR VRIHVDAEGY RAKREESLQR LAVKVAGKVV KYRKNMTLEP
MNAYERHVIH SALQEYPGVT TYSTGVEPNR RTVVAYAPDQ R
//
