ID A0A268TQG4_9HELI Unreviewed; 479 AA.
AC A0A268TQG4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BKH46_05900 {ECO:0000313|EMBL:PAF46969.1};
OS Helicobacter sp. 12S02634-8.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1476199 {ECO:0000313|EMBL:PAF46969.1, ECO:0000313|Proteomes:UP000216003};
RN [1] {ECO:0000313|EMBL:PAF46969.1, ECO:0000313|Proteomes:UP000216003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12S02634-8 {ECO:0000313|EMBL:PAF46969.1,
RC ECO:0000313|Proteomes:UP000216003};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(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: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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02078}.
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:PAF46969.1}.
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DR EMBL; MLAP01000007; PAF46969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268TQG4; -.
DR OrthoDB; 9786339at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000216003; 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 NCBIfam; TIGR01695; murJ_mviN; 1.
DR PANTHER; PTHR43486; LIPID II FLIPPASE MURJ-RELATED; 1.
DR PANTHER; PTHR43486:SF1; LIPID II FLIPPASE MURJ-RELATED; 1.
DR Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
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 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 118..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 174..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 322..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 418..435
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 455..476
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 479 AA; 53456 MW; 926CA05961C62420 CRC64;
MLKKAFLTNS SGIMCSRVFG FLRDLYTAHI LGAGMYSDIF FIAFKFPNLF RRIFGEGAFA
QSFLPSFISS QKKGAFALSV LGIFACVLLV LGLLVWAFSE EVTQLLAFGF DRELIALAQP
IVVINFWYLE LVFIVTFLST LLQYKHSFWV GAYNTALLNI CMIGALYIGR DRDLLQIVYF
LSYGVLCGGV AQILIHIYPL YRWGFFKLFC VGFGHLKRLL SPSSAPIHLR KQTQNDLKSF
FKQFFPAVLG SSTAQIASFI DTMLASFLAS GSISYLYYAN RIFQLPLALF AIAIATALFP
MVAKAIKNAQ THQALKSMKK SFWFLFVMLW GCLIGGIMLK NEIIWLLFEG GSFHRSDTLM
TANVFAMYMI GLLPFGLSRI FSLWLYAHKL QGKAAKISAI SLVFGVVCSL ALMWDFGAVG
LAIASSLSGV MLFVLSVREF GLRKFWGIMA FPKGWLALLV LGVAEVVVLG GFLHFFHIA
//
