GenomeNet

Database: UniProt
Entry: V2XZ91_9FIRM
LinkDB: V2XZ91_9FIRM
Original site: V2XZ91_9FIRM 
ID   V2XZ91_9FIRM            Unreviewed;       331 AA.
AC   V2XZ91;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=N510_002132 {ECO:0000313|EMBL:USF27186.1}, N510_01068
GN   {ECO:0000313|EMBL:ESL15034.1};
OS   Firmicutes bacterium ASF500.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL15034.1};
RN   [1] {ECO:0000313|EMBL:ESL15034.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF500 {ECO:0000313|EMBL:ESL15034.1};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
RN   [2] {ECO:0000313|EMBL:USF27186.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF500 {ECO:0000313|EMBL:USF27186.1};
RA   Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA   Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT   "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT   Model to Study Microbiome Function.";
RL   Submitted (MAY-2022) 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   ---------------------------------------------------------------------------
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; AYJP01000005; ESL15034.1; -; Genomic_DNA.
DR   EMBL; CP097573; USF27186.1; -; Genomic_DNA.
DR   AlphaFoldDB; V2XZ91; -.
DR   STRING; 1378168.N510_01068; -.
DR   PATRIC; fig|1378168.3.peg.1114; -.
DR   eggNOG; COG1847; Bacteria.
DR   HOGENOM; CLU_042512_0_0_9; -.
DR   OrthoDB; 9794483at2; -.
DR   Proteomes; UP000017395; 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   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:UP000017395};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00867}.
FT   DOMAIN          262..328
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          62..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  36472 MW;  17AED48B338828D2 CRC64;
     MLKWIETTGR SEQDAISAAL FQLGLERDDV SVEVIERAKS GFLGFGSNPA KVRVSYEEID
     GKPCPLAEEG EKEAPKEAQE PPKTPTPAVE ETALPAAPMK KPASPALKEE KKEPAPGAEE
     TILAAKPGMA PPKRSQPRQE RRPRPQRENR LQEGDEVLIG SPAPAPKAPV TYEPAAEDDE
     KAIRIREFLT GLMAHLQVQA SPEIFATSEG GYKVVLQGEN LGAIIGRRGE TLDAIQQLTS
     YSINRGQSKR VRVHVDAEGY RAKREESLQR LAVKVAGKVV KYRRNMTLEP MNAYERHVIH
     TALQDYKGVS TYSTGVEPNR RTVVAYAPHQ K
//
DBGET integrated database retrieval system