ID J9WLW0_MYCIP Unreviewed; 923 AA.
AC J9WLW0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=MIP_05301 {ECO:0000313|EMBL:AFS15572.1};
OS Mycobacterium indicus pranii (strain DSM 45239 / MTCC 9506).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1232724 {ECO:0000313|EMBL:AFS15572.1, ECO:0000313|Proteomes:UP000007329};
RN [1] {ECO:0000313|EMBL:AFS15572.1, ECO:0000313|Proteomes:UP000007329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC 9506 {ECO:0000313|EMBL:AFS15572.1};
RX PubMed=17912347; DOI=10.1371/journal.pone.0000968;
RA Ahmed N., Saini V., Raghuvanshi S., Khurana J.P., Tyagi A.K., Tyagi A.K.,
RA Hasnain S.E.;
RT "Molecular analysis of a leprosy immunotherapeutic bacillus provides
RT insights into Mycobacterium evolution.";
RL PLoS ONE 2:E968-E968(2007).
RN [2] {ECO:0000313|EMBL:AFS15572.1, ECO:0000313|Proteomes:UP000007329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45239 / MTCC 9506 {ECO:0000313|Proteomes:UP000007329};
RX PubMed=22965120; DOI=10.1093/nar/gks793;
RA Saini V., Raghuvanshi S., Khurana J.P., Ahmed N., Hasnain S.E., Tyagi A.K.,
RA Tyagi A.K.;
RT "Massive gene acquisitions in Mycobacterium indicus pranii provide a
RT perspective on mycobacterial evolution.";
RL Nucleic Acids Res. 40:10832-10850(2012).
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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP002275; AFS15572.1; -; Genomic_DNA.
DR RefSeq; WP_014942591.1; NC_018612.1.
DR AlphaFoldDB; J9WLW0; -.
DR KEGG; mid:MIP_05301; -.
DR PATRIC; fig|1232724.3.peg.3608; -.
DR HOGENOM; CLU_006301_9_2_11; -.
DR Proteomes; UP000007329; Chromosome.
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; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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}.
FT DOMAIN 419..590
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 34..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428..435
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 478..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 532..535
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 923 AA; 96176 MW; 09A05173A1A8145D CRC64;
MAGKARVHEL AKELGVTSKE VLARLNDQGE FVKSASSTVE APVARRLRES FGGGKPAAEK
APAKAAKGDA KAPDKAPDKS LDAALDNAIN KPAGNGEATA TPAQPGGAAP AAAAQASGAA
PSDAPARPGP APARPSAPSP GQPKPPAPGQ APHPGMTPGP RPGPIPKPRA PRVGNNPFSS
AQPVDRPIPR PAAPRPGAPR PGAPRPGASP GNMPPRPAGA AGQGRPPRPG APRPGGGRPG
GPGGRDGGGG NYRGGGGGVG APPGGGGGFR GRPGGGGGRP GQRGGAAGAF GRPGGAPRRG
RKSKRAKRAE YENMQAPVVG GVRLPHGNGE TIRLARGASL SDFADKINAN PASLVQALFN
LGEMVTATQS VGDETLELLG SEMNYVVQVV SPEDEDRELL ESFDLTYGED EGTEEDLQTR
PPVVTVMGHV DHGKTRLLDT IRKANVREAE AGGITQHIGA YQVSVEHDGD ERPITFIDTP
GHEAFTAMRA RGAKATDIAI LVVAADDGVM PQTVEAINHA QAADVPIVVA VNKIDVEGAD
PAKIRGQLTE YGLVAEDFGG ETMFVDISAK QGTNIDALLE AVLLTADAAL DLRANPDMEA
QGVAIEAHLD RGRGPVATVL VQRGTLRVGD SVVAGDAYGR VRRMVDEHGD DVEEALPSRP
VQVIGFTSVP GAGDNLLVVD EDRIARQIAD KRSARKRNAL AARSRKRISL EDLDSALKET
SQLNLILKGD NAGTVEALEE ALMGIQIDDE VALRVIDRGV GGITETNVNL ASASDAVIIG
FNVRAEGKAT ELANREGVEI RYYSVIYQAI DEIEKALRGM LKPIYEENQL GRAEIRAIFR
SSKVGIIAGC MISSGVVRRN AKARLLRDNV VVTENLTINS LRREKDDVTE VREGFECGMT
LGYSDIKEGD IIESYELVQK ERS
//
