ID A0A0F7HAV5_SERFO Unreviewed; 895 AA.
AC A0A0F7HAV5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:AKG69518.1};
GN ORFNames=CRN79_07540 {ECO:0000313|EMBL:ATM75705.1}, H8I91_14825
GN {ECO:0000313|EMBL:MBC3251543.1}, NCTC13193_00565
GN {ECO:0000313|EMBL:VEI62844.1}, WN53_10605
GN {ECO:0000313|EMBL:AKG69518.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG69518.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG69518.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG69518.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ATM75705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_411 {ECO:0000313|EMBL:ATM75705.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000221800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_411 {ECO:0000313|Proteomes:UP000221800};
RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Ott S., Zhao X.,
RA Nagaraj S., Vavikolanu K., Aluvathingal J., Nadendla S., Geyer C.,
RA Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:VEI62844.1, ECO:0000313|Proteomes:UP000270487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13193 {ECO:0000313|EMBL:VEI62844.1,
RC ECO:0000313|Proteomes:UP000270487};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:MBC3251543.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UPMP2131 {ECO:0000313|EMBL:MBC3251543.1};
RA Richter L., Du Plessis E.M., Duvenage S., Allam M., Korsten L.;
RT "Food and environmental bacterial isolates.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP011254; AKG69518.1; -; Genomic_DNA.
DR EMBL; CP023956; ATM75705.1; -; Genomic_DNA.
DR EMBL; JACNYM010000012; MBC3251543.1; -; Genomic_DNA.
DR EMBL; LR134492; VEI62844.1; -; Genomic_DNA.
DR RefSeq; WP_021807516.1; NZ_SUPV01000019.1.
DR STRING; 47917.AV650_05965; -.
DR GeneID; 30320616; -.
DR KEGG; sfw:WN53_10605; -.
DR PATRIC; fig|47917.8.peg.2189; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000034699; Chromosome.
DR Proteomes; UP000221800; Chromosome.
DR Proteomes; UP000270487; Chromosome 1.
DR Proteomes; UP000596701; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 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:UP000034699}.
FT DOMAIN 394..563
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..545
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 57..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 449..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 503..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 895 AA; 97884 MW; 35CDCBAD377B68D5 CRC64;
MTTDVTVKSL AAEIQTPVDR LVQQFADAGI NKSETDSVTQ HEKETLLAHL NREHGSAPSK
LTLQRKTRST LNIPSTGGKS KSVQIEVRKK RTYVNRDPQE AQQAEAAEQA QREAEEQARR
EAEELAKREA EAKRAAEEQA KREAAEIAKR NSAEKEKVTN QHTDEMTKPA QAEKARREAE
AAELKRKAEE EVRRKVEEDA KRVAEEARRM AEENGEKWAE AEAASAAVET ADYHVTTSEH
ARAAEDENDA KVEGERRSRT RGGKATKQKK GNKLSESKAD REEARTMTRG GKGKRKPSTL
QQGFNKPAQV VNRDVVIGET ITVAELANKM AVKGSQVIKA MMKLGAMATI NQVIDQETAQ
LVAEEMGHKV ILRRENELEE ALMSDRDTGA GAESRAPVVT IMGHVDHGKT SLLDYIRSTK
VAVGEAGGIT QHIGAYHVET ENGMITFLDT PGHAAFTSMR ARGAQATDIV VLVVAADDGV
MPQTIEAIQH AQAAKVPLVV AVNKIDKPEA DPDRVKQELS QYGVMPEEWG GEAQFVHVSA
KAGTGIDELL NAILLQAEVL ELKAVRSGMA SGVVIESFLD KGRGPVATVL VQEGTLNKGD
IVLCGFEYGR VRAMRDELGR EVTSAGPSIP VEILGLSSVP AAGDEATVVR DEKKAREVAL
YRQGKFREVK LARQQKSKLE NMFANMTEGE VSELNIVLKT DVQGTCEAIS DSLQKLSTDE
VKVKIVGSGV GGITETDATL AAASNAIILG FNVRADASAR RVIESESLDL RYYSVIYNLI
DEVKQAMSGM LAPEYKQQII GLAEVRDVFK SPKFGAVAGC MVTEGNIKRH NPIRVLRDNV
VIYEGELESL RRFKDDVNEV RNGMECGIGV KNYNDVRVGD MIEVFEIIEI QRTIA
//
