ID A0A329ZLL5_9HELI Unreviewed; 155 AA.
AC A0A329ZLL5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Small ribosomal subunit protein uS7 {ECO:0000256|HAMAP-Rule:MF_00480};
GN Name=rpsG {ECO:0000256|HAMAP-Rule:MF_00480};
GN ORFNames=CCY97_00100 {ECO:0000313|EMBL:RAX56246.1};
OS Helicobacter sp. 10-6591.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2004998 {ECO:0000313|EMBL:RAX56246.1, ECO:0000313|Proteomes:UP000251062};
RN [1] {ECO:0000313|EMBL:RAX56246.1, ECO:0000313|Proteomes:UP000251062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-6591 {ECO:0000313|EMBL:RAX56246.1,
RC ECO:0000313|Proteomes:UP000251062};
RX PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA Marini R.P., Fox J.G.;
RT "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT necrotizing factor (CNF) colonize laboratory macaques.";
RL Gut Pathog. 9:71-71(2017).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the head domain of the 30S
CC subunit. Is located at the subunit interface close to the decoding
CC center, probably blocks exit of the E-site tRNA. {ECO:0000256|HAMAP-
CC Rule:MF_00480}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 and
CC S11. {ECO:0000256|HAMAP-Rule:MF_00480}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000256|ARBA:ARBA00007151, ECO:0000256|HAMAP-Rule:MF_00480,
CC ECO:0000256|RuleBase:RU003619}.
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:RAX56246.1}.
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DR EMBL; NHYK01000001; RAX56246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329ZLL5; -.
DR OrthoDB; 9807653at2; -.
DR Proteomes; UP000251062; Unassembled WGS sequence.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd14869; uS7_Bacteria; 1.
DR Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1.
DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR InterPro; IPR000235; Ribosomal_uS7.
DR InterPro; IPR005717; Ribosomal_uS7_bac/org-type.
DR InterPro; IPR020606; Ribosomal_uS7_CS.
DR InterPro; IPR023798; Ribosomal_uS7_dom.
DR InterPro; IPR036823; Ribosomal_uS7_dom_sf.
DR NCBIfam; TIGR01029; rpsG_bact; 1.
DR PANTHER; PTHR11205:SF19; 28S RIBOSOMAL PROTEIN S7, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; Ribosomal protein S7; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000251062};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00480};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00480};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00480};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00480}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00480}.
FT DOMAIN 2..148
FT /note="Small ribosomal subunit protein uS7"
FT /evidence="ECO:0000259|Pfam:PF00177"
SQ SEQUENCE 155 AA; 18004 MW; 0C0B42B170CE1EFE CRC64;
MRRRKAPVRE ILGDPIYGNK VVTKFVNKMM YDGKKSVSKK IIYAAFNKIE EKSGEKGIDV
FERALDKVKP LVEVRSRRVG GATYQVPVEV RHARQQSLSI RWILEATRKR NERTMVERLA
NELIDATNDR GAAFKKKEDV HKMAEANKAF AHYRW
//