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Database: UniProt
Entry: F5SVK3_9GAMM
LinkDB: F5SVK3_9GAMM
Original site: F5SVK3_9GAMM 
ID   F5SVK3_9GAMM            Unreviewed;       935 AA.
AC   F5SVK3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=MAMP_02877 {ECO:0000313|EMBL:EGL55883.1};
OS   Methylophaga aminisulfidivorans MP.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL55883.1, ECO:0000313|Proteomes:UP000003544};
RN   [1] {ECO:0000313|EMBL:EGL55883.1, ECO:0000313|Proteomes:UP000003544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX   PubMed=21685284; DOI=10.1128/JB.05403-11;
RA   Han G.H., Kim W., Chun J., Kim S.W.;
RT   "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL   J. Bacteriol. 193:4265-4265(2011).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000645}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
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:EGL55883.1}.
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DR   EMBL; AFIG01000001; EGL55883.1; -; Genomic_DNA.
DR   RefSeq; WP_007145769.1; NZ_AFIG01000001.1.
DR   AlphaFoldDB; F5SVK3; -.
DR   STRING; 1026882.MAMP_02877; -.
DR   eggNOG; COG0532; Bacteria.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000003544; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT   DOMAIN          435..604
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          141..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..586
FT                   /note="G-domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   COMPBIAS        141..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         444..451
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         490..494
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         544..547
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   935 AA;  101828 MW;  3008CE9F7D79FF45 CRC64;
     MSDMRVKDLA GTVGITAERL VEQLNEAGIN VSKPDDFITE DQKQTLLQFL QQRHGKSGDG
     ETTTPKKITL KRKSVSEIKL GGAARGGKSV SVEVRKKRTY VKRDEVEDTT NNAEQTPQLS
     VAEQQAAEVA RLEALRLEEA KRRQQEDEAR RLRESEEEAA AVAAAIEAEN KASEEAKLAA
     EEERKALEEE AKSKKAEKAI EEKVNPKPKQ TTEKTLSASQ LAHKKLEEAD AKRRAANLAR
     IEAEKALEAK KKAREEEEAL EKEKEKARAA AAEAQAKEQK AGVRKTKDAE AKHNRDKSGR
     KGGRNDDDFE RKELHVTEGK GGRRKKKKGG GASKVSVSKD QEHGFSKPTA PVVREVNVPE
     TISVSDLALR MSVKAAEVIK TLMGLGTMAT INQVLDQDTA IIVVEEMGHI AKPILENEVE
     QALQVSDENQ GEAVPRAPVV TVMGHVDHGK TSLLDYIRRT KVTSGEAGGI TQHIGAYKVE
     TSRGQIAFLD TPGHAAFTEM RSRGAKVTDI VILVVAADDG VMPQTIEAIQ HAKAAESMII
     VAVNKIDKQD ANPERVKQEL ANHEVIPEDW GGDVQFIPVS ALTGQGIEDL LEAISIQAEV
     MELKAPEEGP AHGTVIEARL DKGRGTVVTV LVQQGTLNKG DIVVVGQEYG RVRAMFNETG
     EQLNHAGPST PVELLGLSGT PAAGDELQAA PDDRTAREIA NFRQTKAREQ KMAQQQAAKL
     DEMFNKMEEG DVKTLNVVIK GDVHGSVEAV SQGLQKLSTD MVKVRVVGSG VGGINETDAQ
     LAAASDAILI GFNVRADNAA RKVIAEKGLD VQYFSIIYDL LDVVTKAMTG MLEPVYRDEI
     IGLARVDDVF RSPKFGDIAG CLVVEGTVKR NNPIRVLRDN VVVYEGELES LRRFKDDVNE
     VNAGTECGIG VKNYKDVKPG DQIEVYERVL MKPTL
//
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