ID A0A0A0DGA1_9STRE Unreviewed; 341 AA.
AC A0A0A0DGA1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SSIN_1126 {ECO:0000313|EMBL:KGM37134.1};
OS Streptococcus sinensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=176090 {ECO:0000313|EMBL:KGM37134.1, ECO:0000313|Proteomes:UP000030019};
RN [1] {ECO:0000313|EMBL:KGM37134.1, ECO:0000313|Proteomes:UP000030019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU4 {ECO:0000313|EMBL:KGM37134.1,
RC ECO:0000313|Proteomes:UP000030019};
RA Teng J.L., Huang Y., Tse H., Lau S.K., Woo P.C.;
RL Submitted (JUN-2014) 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:KGM37134.1}.
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DR EMBL; JPEN01000066; KGM37134.1; -; Genomic_DNA.
DR RefSeq; WP_037616637.1; NZ_JPEN01000066.1.
DR AlphaFoldDB; A0A0A0DGA1; -.
DR STRING; 176090.SSIN_1126; -.
DR PATRIC; fig|176090.4.peg.1091; -.
DR eggNOG; COG1847; Bacteria.
DR Proteomes; UP000030019; 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 274..340
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 3..53
FT /note="Jag_N domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00867"
SQ SEQUENCE 341 AA; 38201 MW; 8F837CD630D37DFC CRC64;
MVIFTGESVE EAIQNGLKTL DIPRMRAHIT VVSREKKGFL GLFGKKPAQV DVEPIAETTV
VKANQKAVKG VPEEINAQNE PVQSVSEATV DLGRVVAAIK KVEEEGELVS DEVKAQILKN
DKQANTILEE TGTIDLLKTS QAINETAGQK ETDKVVSFEK AVPRQETPVS DAPAESSFFD
LGIQVEENYD IEEVVANVTE YVQRIVDEMD VEATLSSNYN RRTINMQIDT NEPGRVIGYH
GKVLKALQLL AQNYLYNQYS KSFYISINVN DYVEHRAEVL QSYAQKLAQR ALEDRRSQHT
DPMSNNERKI IHRIISRIDG VTSYSEGDEP NRYVVVDIDS E
//
