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Database: UniProt
Entry: A0A4U8SMY1_9HELI
LinkDB: A0A4U8SMY1_9HELI
Original site: A0A4U8SMY1_9HELI 
ID   A0A4U8SMY1_9HELI        Unreviewed;       522 AA.
AC   A0A4U8SMY1;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   ORFNames=LS69_003580 {ECO:0000313|EMBL:TLD87876.1};
OS   Helicobacter sp. MIT 05-5294.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1548150 {ECO:0000313|EMBL:TLD87876.1, ECO:0000313|Proteomes:UP000029926};
RN   [1] {ECO:0000313|EMBL:TLD87876.1, ECO:0000313|Proteomes:UP000029926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 05-5294 {ECO:0000313|EMBL:TLD87876.1,
RC   ECO:0000313|Proteomes:UP000029926};
RX   PubMed=25428971;
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Draft genome sequences of eight enterohepatic helicobacter species
RT   isolated from both laboratory and wild rodents.";
RL   Genome Announc. 2:e01218-e01214(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 membrane {ECO:0000256|HAMAP-Rule:MF_02078};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02078}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000256|HAMAP-
CC       Rule:MF_02078, ECO:0000256|PIRNR:PIRNR002869}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TLD87876.1}.
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DR   EMBL; JRPA02000004; TLD87876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U8SMY1; -.
DR   OrthoDB; 9786339at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029926; Unassembled WGS sequence.
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   PANTHER; PTHR43486; LIPID II FLIPPASE MURJ-RELATED; 1.
DR   PANTHER; PTHR43486:SF1; LIPID II FLIPPASE MURJ-RELATED; 1.
DR   Pfam; PF03023; MurJ; 2.
DR   PIRSF; PIRSF002869; MviN; 2.
DR   PRINTS; PR01806; VIRFACTRMVIN.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02078};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
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|HAMAP-Rule:MF_02078,
KW   ECO:0000256|PIRNR:PIRNR002869};
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        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        76..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        121..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        180..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        328..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        366..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        402..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        436..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        462..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        497..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   522 AA;  58776 MW;  11917B279B4BE3B0 CRC64;
     MFLKAFFTNS SGILTSRILG FFRDLLTATI LGSSIYSDMF FVAFKLPNLF RRVFGEGAFN
     QAFLPGFFNA TLRGGFALKI GLIFCVILLV ISLLVCVFSV PLTKLLAFGF SDELIKLTAP
     LVTINFWYLL LIFIVTLFGA MLQFKRNFTA WAYSPALLNL AMICALLLAR DSESYEAILI
     LSYGVLCGGI AQILLHCYPM WRLGFFRLLW VGVKEIWSVR KNAESKQDSC FGVEEAIRKD
     LLVSENLKNE SKSMESKQDS CLRSAVKKAK WRKETINQSV KRFFKQFSPA MFGSSTAQFA
     SFIDTLLASF LVSGSISCLY YANRIFQLPL AIFAIATSTA LFPLVAKYIK ESKESLALKE
     LSRSFWLLSI LLSLCVVGGL MLQNEIIWLL FERGKFTRQD TLICASVFGA YLIGLLPFGL
     ARIFSLWLYS KSLQSLAAKI SAFSLAVGTF CSFILMQYFG AIGLALGGSI SGFFVFFLTL
     HFFGWNRFWN ILWNPKWILS LVLILATEFL LLLGFKTYIF SL
//
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