MURJ_SYNY3
ID MURJ_SYNY3 Reviewed; 533 AA.
AC Q55179;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000255|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078}; Synonyms=mviN;
GN OrderedLocusNames=slr0488;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 -!- 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}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
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DR EMBL; BA000022; BAA10319.1; -; Genomic_DNA.
DR PIR; S74401; S74401.
DR AlphaFoldDB; Q55179; -.
DR SMR; Q55179; -.
DR STRING; 1148.1001176; -.
DR PaxDb; Q55179; -.
DR EnsemblBacteria; BAA10319; BAA10319; BAA10319.
DR KEGG; syn:slr0488; -.
DR eggNOG; COG0728; Bacteria.
DR InParanoid; Q55179; -.
DR OMA; IFFVAFK; -.
DR PhylomeDB; Q55179; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001425; 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 3: Inferred from homology;
KW 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..533
FT /note="Probable lipid II flippase MurJ"
FT /id="PRO_0000182015"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ SEQUENCE 533 AA; 57053 MW; 00A5B612F744C1D2 CRC64;
MSPSGKSSRS LANIAGIVAI ATLISKVFGL LREQIIAAAF GVGTVVTAYA YAYVIPGFLF
ILLGGINGPF HSALVSVLSK RDREEAAPLV ETVTTLVSGV LLGVTIILVL GAGIFIDLLA
PGLEPETRRM AVQQLQIMAP MALLSGLIGI GFGTLNAADQ YLLPSISPLL SSITVILGLG
VAVWQLGQQL NTEPYWLLGS LLLAGGTTAG AVLQWLAQIV PQAKAGMGKL RLRFNFALPG
VKEVLQVMIP ATLSSGMLYI NFATNLFFAS FIPNAAAAMR YGNFVALTPL GIISNMILVP
FLPVFSRLAD PQDWPELKLR IRQGIMLSAL TMFPLTAILV GLAIPIVQVI YERGAFDAEA
AAEVAPVLAA YGLGMFFYLG RDVLVRVFYA LGDGNSPFKV SLFNIFLNGL LDYLFYKPFG
TVGIVMATVG VNLFSMTIFI WMLNRRLAGL SLGGWAMDLG KLVGVTAIAS VAGWQGSVLW
QRLWGVNSLV ENILEVLTMS SIILVVFTVG VALAKVPEVD LLGDRLWKKF KRV
