Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q1D823

- AGLZ_MYXXD

UniProt

Q1D823 - AGLZ_MYXXD

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Adventurous-gliding motility protein Z

Gene

aglZ

Organism
Myxococcus xanthus (strain DK 1622)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Required for adventurous-gliding motility (A motility), in response to environmental signals sensed by the frz chemosensory system. Forms ordered clusters that span the cell length and that remain stationary relative to the surface across which the cells move, serving as anchor points (focal, transient adhesion sites) that allow the bacterium to move forward. Clusters disassemble at the lagging cell pole.2 Publications

GO - Biological processi

  1. phosphorelay signal transduction system Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Enzyme and pathway databases

BioCyciMXAN246197:GIWU-2964-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Adventurous-gliding motility protein Z
Gene namesi
Name:aglZ
Ordered Locus Names:MXAN_2991
OrganismiMyxococcus xanthus (strain DK 1622)
Taxonomic identifieri246197 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeMyxococcus
ProteomesiUP000002402: Chromosome

Subcellular locationi

Cytoplasm 1 Publication
Note: In motile cells, localizes in ordered clusters spanning the cell length. In stalled cells, localizes at the leading cell pole.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13951395Adventurous-gliding motility protein ZPRO_0000282834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 4814-aspartylphosphatePROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with MglA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
frzCDQ1D4V74EBI-1574592,EBI-6407529

Protein-protein interaction databases

IntActiQ1D823. 13 interactions.
MINTiMINT-7718200.
STRINGi246197.MXAN_2991.

Structurei

3D structure databases

ProteinModelPortaliQ1D823.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 122119Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili213 – 911699Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi123 – 21290Pro-richAdd
BLAST
Compositional biasi1095 – 1361267Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
OMAiREEQNKF.
OrthoDBiEOG6PS5T9.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1D823-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERRVLIVES EHDFALSMAT VLKGAGYQTA LAETAADAQR ELEKRRPDLV
60 70 80 90 100
VLRAELKDQS GFVLCGNIKK GKWGQNLKVL LLSSESGVDG LAQHRQTPQA
110 120 130 140 150
ADGYLAIPFE MGELAALSHG IVPPGTDDTG ASLDAALNGT REAPPPMPPS
160 170 180 190 200
LKAAAGGPPK LPKRERRSAM TEEDRAFLDR TFQSIADRKA ELLAESRQLK
210 220 230 240 250
RPPPRRELMG TPEGKIQILR DELKTREAQL ARLSEIWNVR ERELLSGEDR
260 270 280 290 300
IHEKDVELQG LKMQVDDLLR RFNEAQQATI QKEREHGATV DDLLLQKFSA
310 320 330 340 350
EKDLIEVVAS KEKDINLLRR EVSRAEEELS RRAGELEHGR NEYDKLEKHL
360 370 380 390 400
GVVTLEFEVK EQKLQDTVLA NEGEIARLTK RGDDFEAELN RTISERDQRF
410 420 430 440 450
AELDGEIQAL QERLQQTEQE RDTTVRGLEA RAARAEEHGT QADAEIHRLN
460 470 480 490 500
AERDALEAKL SQQVADLEAD LARTMGERDQ LRLDKDAQEA ELTQRIEERD
510 520 530 540 550
AKLGTLEREL SETIARNEHT EAELNANIQQ QLERIGELEG EVEAVKTHLE
560 570 580 590 600
DRENELTAEL QALGQAKDEL ETDLNDRLQA LSQAKDALEA DLSRQLEELR
610 620 630 640 650
SAKAELEADL TGQIQALTSQ LEETQRQLDD SQRTGEQLSA RVAQLEDTVS
660 670 680 690 700
QRESTIESLQ GDVAARDQRI SELSGDLEAT SQTLAQTQQT LAQTEQQLAD
710 720 730 740 750
TQNTLASTEG ALAETRGELD ATSQTLQQTQ QTLAQTEGAL AETRGELDAT
760 770 780 790 800
SQTLAQTQQT LAQTEQQLAD TQNTLASTEG TLAETRGELE ATSQTLQQTH
810 820 830 840 850
AALEDTRGAL QETSDTLAHT TRERDQRIAE LADLGAAKDA LEQELTGQIG
860 870 880 890 900
HLRSELSETQ GNYEAERAAH EKLAAESSAH IGDLTSERDG LRSELEATSQ
910 920 930 940 950
TLEQTHGQLA ATRDALAREQ HAHQESRKAA ASTQTTLEGQ LAEARAHGED
960 970 980 990 1000
LGEHLTLTKH ELGTRVAELT QLTATLAQTE NTRAHLEERL HTLTEESQRR
1010 1020 1030 1040 1050
EELLQNDLTQ KGTELSDTLR KLTHVTQEKM RQAEVLNREV ATRTEQLKAM
1060 1070 1080 1090 1100
EAKLQTQATE ARRQAEGLGQ QITGLNEQLE QGRKALAGRE DQLRAAGAAQ
1110 1120 1130 1140 1150
QKLTAERDGL AGQLQQAEAR LQQQAQQANQ ERADAKRAAD ELAAKLAKTE
1160 1170 1180 1190 1200
QRITQFAQDA QTQATEADAR AKDLQGQLSA RAKKIQDLEL AVENAQGAKS
1210 1220 1230 1240 1250
RAEKELNAKV AAAESKAHEA STRLAAAQKE RKDLEARHAK EQEDLAAKQK
1260 1270 1280 1290 1300
AELERRDAIK AQEVARLQQS VQEKSKALKV AELELARYKS KSATTATPAK
1310 1320 1330 1340 1350
AAAKPAAAED DELAVRTQLN QVIAPAAAAQ APAPAKKPAA KPAAQAPAKK
1360 1370 1380 1390
APAPAPAPPA ALSDESEPTD RTLVIQLPTA KEDDDWTALV DELDK
Length:1,395
Mass (Da):153,616
Last modified:July 11, 2006 - v1
Checksum:i5E20D7DC3181E36A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti763 – 7631Q → R in AAR39422. (PubMed:15342587)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY487937 Genomic DNA. Translation: AAR39422.1.
CP000113 Genomic DNA. Translation: ABF92300.1.
RefSeqiYP_631200.1. NC_008095.1.

Genome annotation databases

EnsemblBacteriaiABF92300; ABF92300; MXAN_2991.
GeneIDi4106990.
KEGGimxa:MXAN_2991.
PATRICi22648533. VBIMyxXan43560_2946.

Cross-referencesi

Web resourcesi

Protein Spotlight

Slip sliding away - Issue 81 of April 2007

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY487937 Genomic DNA. Translation: AAR39422.1 .
CP000113 Genomic DNA. Translation: ABF92300.1 .
RefSeqi YP_631200.1. NC_008095.1.

3D structure databases

ProteinModelPortali Q1D823.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q1D823. 13 interactions.
MINTi MINT-7718200.
STRINGi 246197.MXAN_2991.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF92300 ; ABF92300 ; MXAN_2991 .
GeneIDi 4106990.
KEGGi mxa:MXAN_2991.
PATRICi 22648533. VBIMyxXan43560_2946.

Phylogenomic databases

eggNOGi NOG12793.
OMAi REEQNKF.
OrthoDBi EOG6PS5T9.

Enzyme and pathway databases

BioCyci MXAN246197:GIWU-2964-MONOMER.

Family and domain databases

InterProi IPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view ]
Pfami PF00072. Response_reg. 1 hit.
[Graphical view ]
SMARTi SM00448. REC. 1 hit.
[Graphical view ]
SUPFAMi SSF52172. SSF52172. 1 hit.
PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "AglZ is a filament-forming coiled-coil protein required for adventurous gliding motility of Myxococcus xanthus."
    Yang R., Bartle S., Otto R., Stassinopoulos A.G., Rogers M., Plamann L., Hartzell P.L.
    J. Bacteriol. 186:6168-6178(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MGLA.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DK 1622.
  3. "Evidence that focal adhesion complexes power bacterial gliding motility."
    Mignot T., Shaevitz J.W., Hartzell P.L., Zusman D.R.
    Science 315:853-856(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN A-TYPE GLIDING MOTILITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAGLZ_MYXXD
AccessioniPrimary (citable) accession number: Q1D823
Secondary accession number(s): Q6RW49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 11, 2006
Last modified: October 29, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3