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Database: UniProt
Entry: A0A1M6NJS4_9CLOT
LinkDB: A0A1M6NJS4_9CLOT
Original site: A0A1M6NJS4_9CLOT 
ID   A0A1M6NJS4_9CLOT        Unreviewed;        76 AA.
AC   A0A1M6NJS4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=RNA-binding protein KhpA {ECO:0000256|HAMAP-Rule:MF_00088};
DE   AltName: Full=KH-domain protein A {ECO:0000256|HAMAP-Rule:MF_00088};
GN   Name=khpA {ECO:0000256|HAMAP-Rule:MF_00088};
GN   ORFNames=SAMN02745912_01756 {ECO:0000313|EMBL:SHJ95930.1};
OS   Paramaledivibacter caminithermalis DSM 15212.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Paramaledivibacter.
OX   NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHJ95930.1, ECO:0000313|Proteomes:UP000184465};
RN   [1] {ECO:0000313|EMBL:SHJ95930.1, ECO:0000313|Proteomes:UP000184465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15212 {ECO:0000313|EMBL:SHJ95930.1,
RC   ECO:0000313|Proteomes:UP000184465};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: A probable RNA chaperone. Forms a complex with KhpB 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_00088}.
CC   -!- SUBUNIT: Forms a complex with KhpB. {ECO:0000256|HAMAP-Rule:MF_00088}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088}.
CC   -!- SIMILARITY: Belongs to the KhpA RNA-binding protein family.
CC       {ECO:0000256|HAMAP-Rule:MF_00088}.
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DR   EMBL; FRAG01000017; SHJ95930.1; -; Genomic_DNA.
DR   RefSeq; WP_073149000.1; NZ_FRAG01000017.1.
DR   AlphaFoldDB; A0A1M6NJS4; -.
DR   STRING; 1121301.SAMN02745912_01756; -.
DR   OrthoDB; 9812389at2; -.
DR   Proteomes; UP000184465; 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; cd22533; KH-II_YlqC-like; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_00088; KhpA; 1.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR020627; KhpA.
DR   PANTHER; PTHR34654; UPF0109 PROTEIN SCO5592; 1.
DR   PANTHER; PTHR34654:SF1; UPF0109 PROTEIN TM_1567; 1.
DR   Pfam; PF13083; KhpA-B_KH; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00088, ECO:0000256|PROSITE-
KW   ProRule:PRU00117}.
SQ   SEQUENCE   76 AA;  8290 MW;  B12478D0F94A23D1 CRC64;
     MGELVKIIAK ALVDHPEEVQ VNEIEGTQSV IIELKVASED MGKVIGKQGR IAKAIRTVVK
     AAATRENKRV VVEIIQ
//
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