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Database: UniProt
Entry: B5IQF0_9CYAN
LinkDB: B5IQF0_9CYAN
Original site: B5IQF0_9CYAN 
ID   B5IQF0_9CYAN            Unreviewed;       540 AA.
AC   B5IQF0;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, 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=mviN {ECO:0000313|EMBL:EDY39606.1};
GN   Synonyms=murJ {ECO:0000256|HAMAP-Rule:MF_02078};
GN   ORFNames=CPCC7001_2487 {ECO:0000313|EMBL:EDY39606.1};
OS   Cyanobium sp. PCC 7001.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Cyanobium.
OX   NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY39606.1, ECO:0000313|Proteomes:UP000003950};
RN   [1] {ECO:0000313|EMBL:EDY39606.1, ECO:0000313|Proteomes:UP000003950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY39606.1,
RC   ECO:0000313|Proteomes:UP000003950};
RA   Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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   -!- 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}.
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DR   EMBL; DS990556; EDY39606.1; -; Genomic_DNA.
DR   RefSeq; WP_006911530.1; NZ_DS990556.1.
DR   AlphaFoldDB; B5IQF0; -.
DR   STRING; 180281.CPCC7001_2487; -.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_006797_5_2_3; -.
DR   OrthoDB; 9804143at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000003950; 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-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   PRINTS; PR01806; VIRFACTRMVIN.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02078}; Cell shape {ECO:0000256|HAMAP-Rule:MF_02078};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02078};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02078};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003950};
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}; Transport {ECO:0000256|HAMAP-Rule:MF_02078}.
FT   TRANSMEM        47..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        83..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        131..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        190..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        256..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        357..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        394..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        423..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        468..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT   TRANSMEM        493..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ   SEQUENCE   540 AA;  56219 MW;  46324366CBAF1E05 CRC64;
     MPQSLRRIAL IVAVATAISK VAGLVRQQAI AAAFGVGAAY DAYNYAYVLP GFLLILLGGI
     NGPFHSAMVS VLARRPREQG AHVLAAINTL VGAGLLVVTL ILLVAADPLI TLVGPGLDAE
     RHAIAVVELR WMAPMALFAG LIGLGFGALN AADEFWLPSV SPLLSSVAVI AGLALLWWQL
     GSAITLPENA LIGGVVLAAS TTVGAVLQWL IQLPALARQG LHRFRLVWDW QDPGVREVLQ
     VMGPATLSSG MLQINVFVSL FFASGIPAAA AGLGYANLLV QTPLGLISNA LLVPLLPVYA
     RLTAPGDRPE LVARIRQGLM LSNASMLPLG ALMAALAVPI VALIYERGAF DAGAATLVGQ
     LLMAYGIGMP AYLARDVLVR VFYALGDGVT PFRWSLAGIG LNALFCWAFV GGPTPWGQQL
     LPVLYAGAAG LVLATVAVNL ITCAGLLLAL QVRLHGLPLL AWGRDSGLLL GAALLGAAAA
     WALATYVGWP TGLLGRLLQT GLSGSLGLLV YGLLAHRAGV PEAEQVVSQF SRRLPKLGRR
//
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