MURJ_VIBCH
ID MURJ_VIBCH Reviewed; 525 AA.
AC O34238; Q9KU49;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable lipid II flippase MurJ {ECO:0000255|HAMAP-Rule:MF_02078};
GN Name=murJ {ECO:0000255|HAMAP-Rule:MF_02078}; Synonyms=mviN;
GN OrderedLocusNames=VC_0680;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=9457888; DOI=10.1128/jb.180.3.762-765.1998;
RA Williams S.G., Carmel-Harel O., Manning P.A.;
RT "A functional homolog of Escherichia coli NhaR in Vibrio cholerae.";
RL J. Bacteriol. 180:762-765(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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:0000255|HAMAP-Rule:MF_02078}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02078}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02078}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000255|HAMAP-
CC Rule:MF_02078}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05373.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ002395; CAA05373.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE003852; AAF93845.1; -; Genomic_DNA.
DR PIR; B82293; B82293.
DR RefSeq; NP_230329.1; NC_002505.1.
DR AlphaFoldDB; O34238; -.
DR SMR; O34238; -.
DR STRING; 243277.VC_0680; -.
DR DNASU; 2615469; -.
DR EnsemblBacteria; AAF93845; AAF93845; VC_0680.
DR KEGG; vch:VC_0680; -.
DR PATRIC; fig|243277.26.peg.652; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_3_6; -.
DR OMA; IFFVAFK; -.
DR BioCyc; VCHO:VC0680-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0034204; P:lipid translocation; IBA:GO_Central.
DR GO; GO:0015836; P:lipid-linked peptidoglycan transport; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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 Pfam; PF03023; MurJ; 1.
DR PIRSF; PIRSF002869; MviN; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
DR TIGRFAMs; TIGR01695; murJ_mviN; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..525
FT /note="Probable lipid II flippase MurJ"
FT /id="PRO_0000182018"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02078"
SQ SEQUENCE 525 AA; 57153 MW; 323D03C33F2C0C53 CRC64;
MFEVTVSKRL LKSGIIVSAM TLISRVLGLV RDVVVANLMG AGASADVFFF ANRIPNFLRR
LFAEGAFSQA FVPVLTEYHA SGDINKTRDL IARASGTLGV LVTIVTLIGV LGSGAVTALF
GAGWFLDWLN GGPAAGKFEL ASLLLKITFP YLWFITFVAL SGAILNTLGK FAVSSFTPVF
LNVMMILCAW YLSPNLEQPE VGLAIGVFLG GLVQFLFQLP FLIKAGVLVR PKWGWKDPGV
VKIRTLMIPA LFGVSVSQIN LLFDSFVASF LQTGSISWLY YSDRLLEFPL GLFGIAIATV
ILPALSRKHV DAHSDGFAHT MDWGIRMVTF LGIPAMLGLM VLAKPMLMVL FMRGEFTPSD
VEQASYSLLA YSSGLLSFML IKVLAPGYYS RQDTKTPVRY GIIAMVSNIV LNAIFAWFYG
YVGLAVATSM SAFLNMALLY RGLHLQGVYH LTRKTVWFVA RLAMAGAVMT GALLWQLDTM
ATWLSWGISQ RALTLTGLIG LGVASYLAIL LLLGVRLKDL KAATE
