P37624

PR
Gene name
rbbA
Protein name
Ribosome-associated ATPase
Names
Ribosomal bound ATPase
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b3486
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

487-556 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P37624

Entry ID Method Resolution Chain Position Source
AF-P37624-F1 Predicted AlphaFoldDB

No variants for P37624

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P37624

No associated diseases with P37624

7 regional properties for P37624

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 13 - 248 IPR003439-1
domain ABC transporter-like, ATP-binding domain 277 - 507 IPR003439-2
domain AAA+ ATPase domain 37 - 225 IPR003593-1
domain AAA+ ATPase domain 301 - 558 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 569 - 903 IPR013525
conserved_site ABC transporter-like, conserved site 148 - 162 IPR017871
domain ABC-2 type transporter, transmembrane domain, bacterial-type 683 - 909 IPR047817

Functions

Description
EC Number
Subcellular Localization
  • Cell inner membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
ATP-binding cassette (ABC) transporter complex A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
cell pole Either of two different areas at opposite ends of an axis of a cell.
cytosolic small ribosomal subunit The small subunit of a ribosome located in the cytosol.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 GO annotations of molecular function

Name Definition
ABC-type transporter activity Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ribosomal small subunit binding Binding to a small ribosomal subunit.

1 GO annotations of biological process

Name Definition
positive regulation of translation Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTHLELVPVP PVAQLAGVSQ HYGKTVALNN ITLDIPARCM VGLIGPDGVG KSSLLSLISG
70 80 90 100 110 120
ARVIEQGNVM VLGGDMRDPK HRRDVCPRIA WMPQGLGKNL YHTLSVYENV DFFARLFGHD
130 140 150 160 170 180
KAEREVRINE LLTSTGLAPF RDRPAGKLSG GMKQKLGLCC ALIHDPELLI LDEPTTGVDP
190 200 210 220 230 240
LSRSQFWDLI DSIRQRQSNM SVLVATAYME EAERFDWLVA MNAGEVLATG SAEELRQQTQ
250 260 270 280 290 300
SATLEEAFIN LLPQAQRQAH QAVVIPPYQP ENAEIAIEAR DLTMRFGSFV AVDHVNFRIP
310 320 330 340 350 360
RGEIFGFLGS NGCGKSTTMK MLTGLLPASE GEAWLFGQPV DPKDIDTRRR VGYMSQAFSL
370 380 390 400 410 420
YNELTVRQNL ELHARLFHIP EAEIPARVAE MSERFKLNDV EDILPESLPL GIRQRLSLAV
430 440 450 460 470 480
AVIHRPEMLI LDEPTSGVDP VARDMFWQLM VDLSRQDKVT IFISTHFMNE AERCDRISLM
490 500 510 520 530 540
HAGKVLASGT PQELVEKRGA ASLEEAFIAY LQEAAGQSNE AEAPPVVHDT THAPRQGFSL
550 560 570 580 590 600
RRLFSYSRRE ALELRRDPVR STLALMGTVI LMLIMGYGIS MDVENLRFAV LDRDQTVSSQ
610 620 630 640 650 660
AWTLNLSGSR YFIEQPPLTS YDELDRRMRA GDITVAIEIP PNFGRDIARG TPVELGVWID
670 680 690 700 710 720
GAMPSRAETV KGYVQAMHQS WLQDVASRQS TPASQSGLMN IETRYRYNPD VKSLPAIVPA
730 740 750 760 770 780
VIPLLLMMIP SMLSALSVVR EKELGSIINL YVTPTTRSEF LLGKQLPYIA LGMLNFFLLC
790 800 810 820 830 840
GLSVFVFGVP HKGSFLTLTL AALLYIIIAT GMGLLISTFM KSQIAAIFGT AIITLIPATQ
850 860 870 880 890 900
FSGMIDPVAS LEGPGRWIGE VYPTSHFLTI ARGTFSKALD LTDLWQLFIP LLIAIPLVMG
910
LSILLLKKQE G