MURJ_THEAB
ID MURJ_THEAB Reviewed; 475 AA.
AC B7IE18;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Lipid II flippase MurJ {ECO:0000305};
GN Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000303|PubMed:28024149};
GN Synonyms=mviN {ECO:0000312|EMBL:ACJ76245.1};
GN OrderedLocusNames=THA_1814 {ECO:0000312|EMBL:ACJ76245.1};
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=484019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B;
RX PubMed=19124572; DOI=10.1128/jb.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND MUTAGENESIS OF SER-17; ARG-18; ARG-24; ARG-52; GLU-57;
RP ASN-162; GLN-229; ASN-231; ARG-255; PHE-256 AND LEU-259.
RC STRAIN=TCF52B;
RX PubMed=28024149; DOI=10.1038/nsmb.3346;
RA Kuk A.C., Mashalidis E.H., Lee S.Y.;
RT "Crystal structure of the MOP flippase MurJ in an inward-facing
RT conformation.";
RL Nat. Struct. Mol. Biol. 24:171-176(2017).
CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid-
CC linked peptidoglycan precursors from the inner to the outer leaflet of
CC the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078,
CC ECO:0000305|PubMed:28024149}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02078, ECO:0000269|PubMed:28024149}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:28024149}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
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DR EMBL; CP001185; ACJ76245.1; -; Genomic_DNA.
DR RefSeq; WP_012580438.1; NC_011653.1.
DR PDB; 5T77; X-ray; 2.00 A; A=1-475.
DR PDB; 6NC6; X-ray; 3.20 A; A/B=1-475.
DR PDB; 6NC7; X-ray; 3.00 A; A/B=1-475.
DR PDB; 6NC8; X-ray; 2.60 A; A=1-475.
DR PDB; 6NC9; X-ray; 1.80 A; A=1-475.
DR PDBsum; 5T77; -.
DR PDBsum; 6NC6; -.
DR PDBsum; 6NC7; -.
DR PDBsum; 6NC8; -.
DR PDBsum; 6NC9; -.
DR AlphaFoldDB; B7IE18; -.
DR SMR; B7IE18; -.
DR STRING; 484019.THA_1814; -.
DR TCDB; 2.A.66.4.8; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR EnsemblBacteria; ACJ76245; ACJ76245; THA_1814.
DR KEGG; taf:THA_1814; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_0_0; -.
DR OMA; IFFVAFK; -.
DR OrthoDB; 749401at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002453; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd13123; MATE_MurJ_like; 1.
DR HAMAP; MF_02078; MurJ_MviN; 1.
DR InterPro; IPR004268; MurJ.
DR Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
DR TIGRFAMs; TIGR01695; murJ_mviN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Lipid II flippase MurJ"
FT /id="PRO_0000439057"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 24..35
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 57..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 100..123
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 145..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 172..175
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 197..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 239..249
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 250..271
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 272..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 309..332
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 354..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 384..386
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 408..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 438..440
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28024149"
FT TOPO_DOM 462..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 17
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 18
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 24
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 52
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 57
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 162
FT /note="N->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 229
FT /note="Q->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 231
FT /note="N->A: Does not affect activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 255
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 256
FT /note="F->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT MUTAGEN 259
FT /note="L->W: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28024149"
FT HELIX 3..31
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 36..56
FT /evidence="ECO:0007829|PDB:6NC9"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 73..100
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:6NC9"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:6NC9"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6NC8"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 247..264
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 283..307
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 361..409
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 414..433
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 442..461
FT /evidence="ECO:0007829|PDB:6NC9"
FT HELIX 463..474
FT /evidence="ECO:0007829|PDB:6NC9"
SQ SEQUENCE 475 AA; 54091 MW; D0814160B5B67A10 CRC64;
MSILFSSILF SIATFFSRIL GLFRDVLFAK YFGVSYELDA YFIAIMFPFF LRKVFGEGAM
SSAFVPLYSE KSGEEKDKFL SSVINGFSLI ILALVILSYF FPELIINLFG AGSSHETKIL
AKKLLLITSP SIYFIFLWAI SYSILNTNNK FFWPALTPSI SNITIIIGTF LSTKYGIISP
TIGFLIGSIL MFFSIIKSII KHKYYFTIKH FPHFLKLFFP TFMTMVVSQI NTVVDMNVVS
FYDKGSISYL QYASRFYLLP YGLFAVSVST VVLSKISNDR KNFNYHLNDA LKTTLFFTIP
SMVGLIFLST PIIRFFYEHG AFTSKDTLIT SKILIAYTLG LPFYGIYSTI SRSYHAIKNT
KTPFIAATIV SLSNIILDII FGLKYGPIGV ALATSIAGII GVLYLLFSVK TFPIKDFLKI
SLNSLIMLFV IYLTDFTDNE FWFLIQILIG ILVYLIFSSI FYRDLIRRFL YARKK
