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
//