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Database: UniProt
Entry: H3NQU7_9FIRM
LinkDB: H3NQU7_9FIRM
Original site: H3NQU7_9FIRM 
ID   H3NQU7_9FIRM            Unreviewed;       330 AA.
AC   H3NQU7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=HMPREF9709_01708 {ECO:0000313|EMBL:EHR32094.1};
OS   Helcococcus kunzii ATCC 51366.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Helcococcus.
OX   NCBI_TaxID=883114 {ECO:0000313|EMBL:EHR32094.1, ECO:0000313|Proteomes:UP000004191};
RN   [1] {ECO:0000313|EMBL:EHR32094.1, ECO:0000313|Proteomes:UP000004191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51366 {ECO:0000313|EMBL:EHR32094.1,
RC   ECO:0000313|Proteomes:UP000004191};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Helcococcus kunzii ATCC 51366.";
RL   Submitted (JAN-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:EHR32094.1}.
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DR   EMBL; AGEI01000031; EHR32094.1; -; Genomic_DNA.
DR   RefSeq; WP_005399223.1; NZ_JH601088.1.
DR   AlphaFoldDB; H3NQU7; -.
DR   STRING; 883114.HMPREF9709_01708; -.
DR   eggNOG; COG1847; Bacteria.
DR   HOGENOM; CLU_042512_0_0_9; -.
DR   OrthoDB; 9794483at2; -.
DR   Proteomes; UP000004191; 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   Reference proteome {ECO:0000313|Proteomes:UP000004191};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00867}.
FT   DOMAIN          264..330
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          5..55
FT                   /note="Jag_N domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00867"
FT   REGION          98..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   330 AA;  37912 MW;  A7FA38C3444F4EB1 CRC64;
     MKSIIKSSKT IEEAVDLGLK ELGLDRNNTE IEIIQEPTKG FLGMFGGNDA IVKIKEKDKS
     TDINLDDIFG DLKQNSSFAE VEDESDEEID ERFSKYDDLE EDEEEIVETE SHDTVDEVVE
     NKEDDSYEDS VDSYEDETTE TEQEEYEIFK SDKEKTVNTR ELTFSGEAVE INDEDSLEVV
     AQKTKKILED ILVKMHIETK VDYETNKNNI INLDLSDISE NDTGIVIGSK GETLNAIQYT
     LSLLVNRNTK QFYRVTLNVA DYRDRRKRSI ENNAKKVAFK VLKTKKSIAL KPMNSYERRI
     VHYALQSYKE IETVSSGKFP NRKVVVKYKG
//
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