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Protein

Leukotoxin translocation ATP-binding protein LktB

Gene

lktB

Organism
Bibersteinia trehalosi (Pasteurella trehalosi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Part of the ABC transporter complex LktBD involved in leukotoxin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).Curated

Catalytic activityi

ATP + H2O + peptide(In) = ADP + phosphate + peptide(Out).

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi503 – 510ATP8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processTransport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Leukotoxin translocation ATP-binding protein LktB (EC:3.6.3.43)
Gene namesi
Name:lktB
OrganismiBibersteinia trehalosi (Pasteurella trehalosi)
Taxonomic identifieri47735 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBibersteinia

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei159 – 179HelicalAdd BLAST21
Transmembranei192 – 212HelicalAdd BLAST21
Transmembranei270 – 290HelicalAdd BLAST21
Transmembranei296 – 316HelicalAdd BLAST21
Transmembranei389 – 409HelicalAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000923881 – 708Leukotoxin translocation ATP-binding protein LktBAdd BLAST708

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ933E0.
SMRiQ933E0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 126Peptidase C39Add BLAST126
Domaini155 – 437ABC transmembrane type-1Add BLAST283
Domaini469 – 704ABC transporterAdd BLAST236

Domaini

In LktB the peptidase C39 domain, the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.1560.10. 1 hit.
InterProiView protein in InterPro
IPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR036640. ABC1_TM_sf.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR010132. ATPase_T1SS_HlyB.
IPR027417. P-loop_NTPase.
IPR005074. Peptidase_C39.
PfamiView protein in Pfam
PF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
PF03412. Peptidase_C39. 1 hit.
SMARTiView protein in SMART
SM00382. AAA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsiTIGR01846. type_I_sec_HlyB. 1 hit.
PROSITEiView protein in PROSITE
PS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
PS50990. PEPTIDASE_C39. 1 hit.

Sequencei

Sequence statusi: Complete.

Q933E0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEANHQRNDL GLVALTMLAQ YHNISLNPEE IKHKFDLDGK GLSLTSWLLA
60 70 80 90 100
AKSLALKAKH IKKEISRLHL VNLPALVWQD NGKHFLLVKV DTDNNRYLTY
110 120 130 140 150
NLEQDAPQIL SQDEFEACYQ GQLILVTSRA SVVGQLAKFD FTWFIPAVIK
160 170 180 190 200
YRKIFLETLI VSIFLQIFAL ITPLFFQVVM DKVLVHRGFS TLNIITVALA
210 220 230 240 250
IVIIFEIVLS GLRTYVFSHS TSRIDVELGA KLFRHLLSLP ISYFENRRVG
260 270 280 290 300
DTVARVRELD QIRNFLTGQA LTSVLDLLFS FIFFAVMWYY SPKLTLVILG
310 320 330 340 350
SLPFYILWSI FISPILRRRL DDKFARSADN QAFLVESVTA INMIKAMAVA
360 370 380 390 400
PQMTDTWDKQ LASYVSSSFR VTVLATIGQQ GVQLIQKTVM VINLWLGAHL
410 420 430 440 450
VISGDLSIGQ LIAFNMLSGQ VIAPVIRLAQ LWQDFQQVGI SVTRLGDVLN
460 470 480 490 500
SPTEQYQGKL SLPEIKGDIS FKNIRFRYKP DAPTILNNVN LEIRQGEVIG
510 520 530 540 550
IVGRSGSGKS TLTKLLQRFY IPENGQVLID GHDLALADPN WLRRQIGVVL
560 570 580 590 600
QDNVLLNRSI RENIALSDPG MPMERVIYAA KLAGAHDFIS ELREGYNTIV
610 620 630 640 650
GEQGAGLSGG QRQRIAIARA LVNNPKILIF DEATSALDYE SEHIIMQNMQ
660 670 680 690 700
KICQGRTVIL IAHRLSTVKN ADRIIVMEKG EIVEQGKHHE LLQNSNGLYS

YLHQLQLN
Length:708
Mass (Da):79,743
Last modified:December 1, 2001 - v1
Checksum:i9CB9FBCEA0A29642
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti351P → S in strain: Serotype T10 / PH252. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314523 Genomic DNA. Translation: AAL12814.1.
AF314524 Genomic DNA. Translation: AAL12817.1.
AF314525 Genomic DNA. Translation: AAL12820.1.
AF314526 Genomic DNA. Translation: AAL12823.1.

Similar proteinsi

Entry informationi

Entry nameiLKTB_BIBTR
AccessioniPrimary (citable) accession number: Q933E0
Secondary accession number(s): Q93FG0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: December 1, 2001
Last modified: October 25, 2017
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Leu-10 is present instead of the conserved Cys which is expected to be the active site residue of peptidase C39. Thus this protein is presumed to be without peptidase activity.Curated

Documents

  1. SIMILARITY comments
    Index of protein domains and families