ID K9RN88_9CYAN Unreviewed; 523 AA.
AC K9RN88;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=Riv7116_6679 {ECO:0000313|EMBL:AFY59001.1};
OS Rivularia sp. PCC 7116.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC Rivularia.
OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY59001.1, ECO:0000313|Proteomes:UP000010380};
RN [1] {ECO:0000313|EMBL:AFY59001.1, ECO:0000313|Proteomes:UP000010380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY59001.1,
RC ECO:0000313|Proteomes:UP000010380};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP003549; AFY59001.1; -; Genomic_DNA.
DR RefSeq; WP_015122550.1; NC_019678.1.
DR AlphaFoldDB; K9RN88; -.
DR STRING; 373994.Riv7116_6679; -.
DR KEGG; riv:Riv7116_6679; -.
DR PATRIC; fig|373994.3.peg.7113; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_2_3; -.
DR OrthoDB; 9804143at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010380; 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 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:UP000010380};
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 48..72
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 84..111
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 155..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 191..218
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 320..346
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 391..410
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 416..438
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 450..471
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 523 AA; 56762 MW; 48802BF9639FD870 CRC64;
MKSRSLKNIA GIVAIATLVS KLFGLLRSTC IAAAFGVGAV ANAFNYAYII PGFLLIVVGG
LNGPLHTALV SILARRDEED SKDLVAAIAT LLTLILIPFT LLIIIFAPFL IDLLAPGLNF
QVREIAILQL QIMAPLALLA GLIGVGVGSL NAADLYWLPS VSPMLSSIAV ISSLGILAWR
LGDEINAPQN LLLGGMVLAA ATLAGALLQW FVQLIVQARF GLLTIRPRFN FRSGEVKQVM
RLMAPATLSA GMSNINLYVD LRFASFIPQA AATLSYAELL SQTPRGLLSS ILLVPLLPSF
SRLAANQEWD QLKEQVRQSI VVTALIILPL SALMMALATP IVKIVYQRQA FDNQAVQMVS
SVLVAYSLGM FPSVGRQILT RVCYALNDAK TPFRISGFNI LLNFGLDYFL VKSFGISGLV
FASMGVNLIA GGMLLIYLHR QLNGLRWREW SLPILGLTLA STITGLTSWV TSLGIERVWQ
AEGLIFDLVQ LSVSAIFGLI IFSLIMVLLR IREVDLLFSR LRR
//
