AGLZ_MYXXD
ID AGLZ_MYXXD Reviewed; 1395 AA.
AC Q1D823; Q6RW49;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Adventurous-gliding motility protein Z;
GN Name=aglZ; OrderedLocusNames=MXAN_2991;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH MGLA.
RX PubMed=15342587; DOI=10.1128/jb.186.18.6168-6178.2004;
RA Yang R., Bartle S., Otto R., Stassinopoulos A.G., Rogers M., Plamann L.,
RA Hartzell P.L.;
RT "AglZ is a filament-forming coiled-coil protein required for adventurous
RT gliding motility of Myxococcus xanthus.";
RL J. Bacteriol. 186:6168-6178(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN [3]
RP ROLE IN A-TYPE GLIDING MOTILITY, AND SUBCELLULAR LOCATION.
RX PubMed=17289998; DOI=10.1126/science.1137223;
RA Mignot T., Shaevitz J.W., Hartzell P.L., Zusman D.R.;
RT "Evidence that focal adhesion complexes power bacterial gliding motility.";
RL Science 315:853-856(2007).
CC -!- FUNCTION: Required for adventurous-gliding motility (A motility), in
CC response to environmental signals sensed by the frz chemosensory
CC system. Forms ordered clusters that span the cell length and that
CC remain stationary relative to the surface across which the cells move,
CC serving as anchor points (focal, transient adhesion sites) that allow
CC the bacterium to move forward. Clusters disassemble at the lagging cell
CC pole. {ECO:0000269|PubMed:15342587, ECO:0000269|PubMed:17289998}.
CC -!- SUBUNIT: Interacts with MglA. {ECO:0000269|PubMed:15342587}.
CC -!- INTERACTION:
CC Q1D823; Q1D4V7: frzCD; NbExp=4; IntAct=EBI-1574592, EBI-6407529;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289998}. Note=In
CC motile cells, localizes in ordered clusters spanning the cell length.
CC In stalled cells, localizes at the leading cell pole.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Slip sliding away - Issue 81
CC of April 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/081";
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DR EMBL; AY487937; AAR39422.1; -; Genomic_DNA.
DR EMBL; CP000113; ABF92300.1; -; Genomic_DNA.
DR RefSeq; WP_011553047.1; NC_008095.1.
DR AlphaFoldDB; Q1D823; -.
DR SMR; Q1D823; -.
DR IntAct; Q1D823; 13.
DR MINT; Q1D823; -.
DR STRING; 246197.MXAN_2991; -.
DR EnsemblBacteria; ABF92300; ABF92300; MXAN_2991.
DR GeneID; 41360353; -.
DR KEGG; mxa:MXAN_2991; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_251724_0_0_7; -.
DR OMA; FIAVYQH; -.
DR OrthoDB; 35321at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Motor protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..1395
FT /note="Adventurous-gliding motility protein Z"
FT /id="PRO_0000282834"
FT DOMAIN 4..122
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 137..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..911
FT /evidence="ECO:0000255"
FT COMPBIAS 1223..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 763
FT /note="Q -> R (in Ref. 1; AAR39422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1395 AA; 153616 MW; 5E20D7DC3181E36A CRC64;
MERRVLIVES EHDFALSMAT VLKGAGYQTA LAETAADAQR ELEKRRPDLV VLRAELKDQS
GFVLCGNIKK GKWGQNLKVL LLSSESGVDG LAQHRQTPQA ADGYLAIPFE MGELAALSHG
IVPPGTDDTG ASLDAALNGT REAPPPMPPS LKAAAGGPPK LPKRERRSAM TEEDRAFLDR
TFQSIADRKA ELLAESRQLK RPPPRRELMG TPEGKIQILR DELKTREAQL ARLSEIWNVR
ERELLSGEDR IHEKDVELQG LKMQVDDLLR RFNEAQQATI QKEREHGATV DDLLLQKFSA
EKDLIEVVAS KEKDINLLRR EVSRAEEELS RRAGELEHGR NEYDKLEKHL GVVTLEFEVK
EQKLQDTVLA NEGEIARLTK RGDDFEAELN RTISERDQRF AELDGEIQAL QERLQQTEQE
RDTTVRGLEA RAARAEEHGT QADAEIHRLN AERDALEAKL SQQVADLEAD LARTMGERDQ
LRLDKDAQEA ELTQRIEERD AKLGTLEREL SETIARNEHT EAELNANIQQ QLERIGELEG
EVEAVKTHLE DRENELTAEL QALGQAKDEL ETDLNDRLQA LSQAKDALEA DLSRQLEELR
SAKAELEADL TGQIQALTSQ LEETQRQLDD SQRTGEQLSA RVAQLEDTVS QRESTIESLQ
GDVAARDQRI SELSGDLEAT SQTLAQTQQT LAQTEQQLAD TQNTLASTEG ALAETRGELD
ATSQTLQQTQ QTLAQTEGAL AETRGELDAT SQTLAQTQQT LAQTEQQLAD TQNTLASTEG
TLAETRGELE ATSQTLQQTH AALEDTRGAL QETSDTLAHT TRERDQRIAE LADLGAAKDA
LEQELTGQIG HLRSELSETQ GNYEAERAAH EKLAAESSAH IGDLTSERDG LRSELEATSQ
TLEQTHGQLA ATRDALAREQ HAHQESRKAA ASTQTTLEGQ LAEARAHGED LGEHLTLTKH
ELGTRVAELT QLTATLAQTE NTRAHLEERL HTLTEESQRR EELLQNDLTQ KGTELSDTLR
KLTHVTQEKM RQAEVLNREV ATRTEQLKAM EAKLQTQATE ARRQAEGLGQ QITGLNEQLE
QGRKALAGRE DQLRAAGAAQ QKLTAERDGL AGQLQQAEAR LQQQAQQANQ ERADAKRAAD
ELAAKLAKTE QRITQFAQDA QTQATEADAR AKDLQGQLSA RAKKIQDLEL AVENAQGAKS
RAEKELNAKV AAAESKAHEA STRLAAAQKE RKDLEARHAK EQEDLAAKQK AELERRDAIK
AQEVARLQQS VQEKSKALKV AELELARYKS KSATTATPAK AAAKPAAAED DELAVRTQLN
QVIAPAAAAQ APAPAKKPAA KPAAQAPAKK APAPAPAPPA ALSDESEPTD RTLVIQLPTA
KEDDDWTALV DELDK
