ID Q2CFQ1_OCEGH Unreviewed; 516 AA.
AC Q2CFQ1;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 08-NOV-2023, entry version 50.
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=OG2516_16961 {ECO:0000313|EMBL:EAR51431.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR51431.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR51431.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAR51431.1}.
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DR EMBL; AAOT01000012; EAR51431.1; -; Genomic_DNA.
DR RefSeq; WP_007256696.1; NZ_CH724109.1.
DR AlphaFoldDB; Q2CFQ1; -.
DR STRING; 314256.OG2516_16961; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_5_0_5; -.
DR OMA; IFFVAFK; -.
DR OrthoDB; 9816572at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003635; 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-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:UP000003635};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 92..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 385..401
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
FT TRANSMEM 407..426
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..503
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02078"
SQ SEQUENCE 516 AA; 55555 MW; 3ED57B64DD4EACCF CRC64;
MQPIKLIAGF LTVGVWTLLS RVLGFVRDIL IAASLGAGPV AEAFLIAFSL PNMFRRFFAE
GAFNMAFVPL FSKKLEEPDE AREFARDAFT GLATVLVVFT VIAVAAMPWL VLAMASGFLG
DERYPLTVIY GRIAFPYILF ISLAALLSGV LNSTGRFVAA AAAPVLLNVM FISALFLGES
LGWPVGDTLI WTVPLAGLAQ LALVWIAASR AGFRLTFRRP RLTPDLRRLA IIAGPAMLAG
GVVQVNLLVG RQVASFFDGA IAWLNYADRL YQLPLGVVGI AVGVVLLPEL SRRLAAGDEQ
GGRESFNRAC EFSLAMTVPA AVALMAIPVP LVSVLFERGA FDSDDTYATA LAVAIYGAGL
PAFVLQKTLQ PLYFAREDTK SPFRFAVVSM LVNAAVAIGL APLVGYAAAA MGTTLAAWSM
VALLWWKSRR MGPAAAFDDR FRRRIWRTVA AALVMGLTLM VAFRLTAPVF DMTLIRYLAL
AGLVALGIAV YFAVGSLFGA FRLSEFTRAM RRRSAT
//