ID K9RXD6_SYNP3 Unreviewed; 560 AA.
AC K9RXD6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN OrderedLocusNames=Syn6312_2642 {ECO:0000313|EMBL:AFY61737.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY61737.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR EMBL; CP003558; AFY61737.1; -; Genomic_DNA.
DR AlphaFoldDB; K9RXD6; -.
DR STRING; 195253.Syn6312_2642; -.
DR KEGG; syne:Syn6312_2642; -.
DR PATRIC; fig|195253.3.peg.2697; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_2_3; -.
DR OrthoDB; 9804143at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010379; Chromosome.
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 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|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 Reference proteome {ECO:0000313|Proteomes:UP000010379};
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 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 84..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 122..148
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 265..290
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 302..326
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 446..465
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 477..499
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 511..534
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 60133 MW; 893CA4136826D2BB CRC64;
MKEKTDPSPS PKDSNSTDNP DGITSTDLGT QPTPTHPSKP VRSLATIATI VAIATLISKL
AGLVRQQAIA AEFGVGAAVD AYNYAYVIPG FLFVLLGGIN GPFHSSIISV VLKHPKEKAA
PLVETVTTLV GGLLLILTGL LILFARPLIQ IIAPGASPDI QAIATEQFQI MAPLAVLSGL
IGIGFGTLNA ADQYWLPSVS PLLSSVTVII GIWFFSHLYG PAVLAWGTLA GGLLQWFVQI
PAQWQAGMGR LRLRFDFNQP EVRELGQLMI PATLSSGMLL ISVYISLFFA SQLPTGAASA
LGYAQLLFLT PLGILSNVIL VPYMPIFSRL ASPPDWPELK QRIRQSLVLT ALSMMPVGAW
MAALALPTVR VIYERYAFDF AASRLVAALL LVYAVGMFAY LARDVLVRVF YGLGDGSTPL
KITLWGLAFN FGFNFFFTRS FGAPGLAMAT VGVNLLSFLA LLWILQRRLG GLPWRDLLWP
LGGVALASVA SGGACWGALQ GLKGVMGTEG LVNQLMQLAV AGLAGVVVFG LMIWPMKLTE
LDFFLAKLYR FLPSNWRRNG
//
