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Database: UniProt
Entry: A0A0S8JTK1_9BACT
LinkDB: A0A0S8JTK1_9BACT
Original site: A0A0S8JTK1_9BACT 
ID   A0A0S8JTK1_9BACT        Unreviewed;       530 AA.
AC   A0A0S8JTK1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 23.
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=AMJ85_02445 {ECO:0000313|EMBL:KPL11966.1};
OS   candidate division BRC1 bacterium SM23_51.
OC   Bacteria; Candidatus Sumerlaeota.
OX   NCBI_TaxID=1703761 {ECO:0000313|EMBL:KPL11966.1, ECO:0000313|Proteomes:UP000051549};
RN   [1] {ECO:0000313|EMBL:KPL11966.1, ECO:0000313|Proteomes:UP000051549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_51 {ECO:0000313|EMBL:KPL11966.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPL11966.1}.
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DR   EMBL; LJUL01000031; KPL11966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8JTK1; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000051549; 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; 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 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};
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        94..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        165..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        192..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        237..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        282..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        317..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        360..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        394..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        492..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   530 AA;  57313 MW;  2D858F7B182BF4EB CRC64;
     MGRRSQVVSA TGLISSLTFA SRILGVVRDS VVAAHLGATR YNDIFQIAFA IPNLARRVLG
     EGALSAFIVP IITGIRRKEG EAAAWRSTCN AFNLFAAITL ALAIVGCLFA KPLFFLYGGA
     RFQFADQPAL FALGGSLTRI MFPYLMFLAL VALLMGVLHS LNHFFAPALG SIVINIVVIA
     AALLFFKVED RQFLYVLAVA VMIGAVIRLL LLFPPLIRRG FRWRPIFDWR EKGFRELASK
     LPAAFYGTAI AQINIAITLN LANWCGEGSV TYLQYSQRLI QLPLALFAAA LSTALLPQLS
     AVVAAGDRRE LRDLMTFAFR AIALAFFPAA IGLMVLGPPI VQVLFQRGAW EEAATKGTAL
     ALLCYAIGLV ALGAQRIFIP LYYAQKDMMT PVKYGAAAMV VNIVLAVALM LIVRAYWPPL
     AFAGLALASS LSASLNGWLL WRGLTRRFGR DLAGPAGSIL LRALLCAAFM GVVCSLGFHA
     SERALHHPTG TAVLFALTVA WVVAGVAVYA IATRAVALWD RQALARLLRR
//
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