ID V6F7Z0_MAGGM Unreviewed; 518 AA.
AC V6F7Z0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=mviN {ECO:0000313|EMBL:CDL00421.1};
GN Synonyms=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN OrderedLocusNames=MGMSRv2__3206 {ECO:0000313|EMBL:CDL00421.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDL00421.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDL00421.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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:0000256|HAMAP-Rule:MF_02078,
CC ECO:0000256|PIRNR:PIRNR002869}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02078}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG794546; CDL00421.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F7Z0; -.
DR STRING; 1430440.MGMSRv2__3206; -.
DR KEGG; mgy:MGMSRv2__3206; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000018922; Chromosome I.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd13123; MATE_MurJ_like; 1.
DR HAMAP; MF_02078; MurJ_MviN; 1.
DR InterPro; IPR004268; MurJ.
DR NCBIfam; TIGR01695; murJ_mviN; 1.
DR PANTHER; PTHR47019; LIPID II FLIPPASE MURJ; 1.
DR PANTHER; PTHR47019:SF1; LIPID II FLIPPASE MURJ; 1.
DR Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02078};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02078,
KW ECO:0000256|PIRNR:PIRNR002869};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02078};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02078}; Reference proteome {ECO:0000313|Proteomes:UP000018922};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02078};
KW Transport {ECO:0000256|HAMAP-Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 88..113
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 133..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 313..337
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 349..366
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 386..404
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 449..467
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 479..506
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 518 AA; 54852 MW; 91553E67BE928D9E CRC64;
MNLIRSIATV GGFTLGSRIT GFARDILIAN YLGAGLVADC FFVAFKFPNL FRRLFAEGAF
NAAFVPLFAG KLEQEGEHAA KRFAENALAV LAVALTAFVA LMEIVMPWAI YVLAPGFDAV
PGKMELAAEL SRITFPYLLF ISLVSLQSGV LNSVGRFAAA AATPILLNLT LMAALIGLTP
LTPTSGHALA IGTTIAGILQ FLWLVYSLKS QGWLLSWRRP HLDADVVLLM KRIVPGAMGA
GIYQVNLLVD TMIASMMAQG AVSYLYYADR INQLPLGVVG IAVGTALLPI LSRQIRAGND
EAAHHSQNRA LEFSLLLTLP AMAAIAVLSV PLVMVLFQRG AFGTVETQAT AGALAAFSLG
LPAYVLAKCL TPAFFARHDT ATPVKLAAAA MIANIVLNLA LWPLGLAQVG IALATALSAW
LNVGLLAWVL RKRGYFRLDA RLRTKAPRII GASVLMAAIV GTAGWWAEPL MAASGQGQRA
LWLAGLVGGG IVLFALLAQL TGAARLGEIK AMVKRQQP
//
