ID A0A0H3GRG5_KLEPH Unreviewed; 511 AA.
AC A0A0H3GRG5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=KPHS_19580 {ECO:0000313|EMBL:AEW60656.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW60656.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW60656.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW60656.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
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; CP003200; AEW60656.1; -; Genomic_DNA.
DR RefSeq; WP_002899104.1; NC_016845.1.
DR RefSeq; YP_005226258.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GRG5; -.
DR STRING; 1125630.KPHS_19580; -.
DR GeneID; 11846976; -.
DR KEGG; kpm:KPHS_19580; -.
DR PATRIC; fig|1125630.4.peg.1908; -.
DR HOGENOM; CLU_006797_5_3_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007841; 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; 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 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|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}; Reference proteome {ECO:0000313|Proteomes:UP000007841};
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 27..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 82..110
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 130..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 188..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 236..259
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 271..288
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 408..429
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 441..466
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 478..501
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 511 AA; 55355 MW; F8B6D57579C76287 CRC64;
MNLLKSLAAV SSMTMFSRVL GFARDAIVAR IFGAGMATDA FFVAFKLPNL LRRIFAEGAF
SQAFVPILAE YKSKQGEDAT RVFVSYVSGL LTLALAIVTV IGMLAAPWVI TITAPGFADT
ADKFALTTQL LRITFPYILL ISLASLVGAI LNTWNRFSVP AFAPTFLNVS MIGFALFAAP
YFHPPVLALA WAVTVGGVLQ LAYQLPHLKK IGMLVLPRIN LKDAGAMRVV KQMGPAILGV
SVSQISLIIN TIFASFLVSG SVSWMYYADR LMEFPSGVLG VALGTILLPS LSKSFASGNH
DEYCRLMDWG LRLCFLLALP SAVALGILAK PLTVALFQYG KFSAFDAAMT QRALVAYSVG
LMGLIVVKVL APGFYSRQDI KTPVKIAIIT LIMTQVMNLA FIGPLKHAGL SLSIGLAACL
NAALLYWQLR KQKIFTPQPG WLAFLLRLII AVLVMAAALL GVMHLMPEWS LGTMPFRLMR
LLAVVIAGVV AYFATLLVLG FRVKEFVRRT A
//
