ID Q4JSD4_CORJK Unreviewed; 1303 AA.
AC Q4JSD4;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:CAI38273.1};
GN OrderedLocusNames=jk2091 {ECO:0000313|EMBL:CAI38273.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI38273.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI38273.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI38273.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CR931997; CAI38273.1; -; Genomic_DNA.
DR STRING; 306537.jk2091; -.
DR KEGG; cjk:jk2091; -.
DR PATRIC; fig|306537.10.peg.2121; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_0_1_11; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd13123; MATE_MurJ_like; 1.
DR CDD; cd13973; PK_MviN-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR004268; MurJ.
DR PANTHER; PTHR47019; LIPID II FLIPPASE MURJ; 1.
DR PANTHER; PTHR47019:SF1; LIPID II FLIPPASE MURJ; 1.
DR Pfam; PF03023; MurJ; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 573..595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1009..1033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 136779 MW; 769178D3A83C37E0 CRC64;
MLHKDGVVTS EQEREDQPAS PSAGQRGRFR ATQPPALAPK KDRAKTEMSA GGHGASQSPA
EVAPTSRNGQ GSQSGQGGQS NGAHNGSDAA AVQGAKSTAA TAGTATAASA SATATAADEP
TGNGANTGGN AGSTGNSGTG GSTDGQSQKQ SDEQIVRAGG SMAIATLISR ITGFLRTVFI
ASALGGAVAS AFNTANTLPN LVTELVLGAV LTSLVVPVLV RAEKEDADHG EAFIRRLLTL
TFSLTLVITL VSVACAPLLV RMSLDSEGHV NIGMSTAFAY LVLPQIMFYA MFAVFMAILN
TKGVFKPGAW APVANNVVTL AVLGLYMFLP RDTKLQPTDN VTITDPHVML LGLGTTAGVV
MQALIMVPFL RKAGINLRPL WGIDERLKSF GGMAIAIVVY VAISQVGWLL NNRIASDTWE
VAPTIYMQAW QLLQMPYGVI GVTLLTAVMP RLSRNAAEGD DKAVVRDLTV ASKLTMLAMV
PIIVFFTCFG TLISAALFAY KEFSLEDANV LGWTISFSAF TLIPYALVLL HLRVFYAREE
VWTPTFIIAG ITATKLTFAY IAPQIATEPR LVVVLLGAAN GLGFMAGAII GDRLLRRSLG
DLQFRKVTMT VLWALGSSLI GALVAWRVDV LLTHFAFQTL ANPWFIIRLL IAGVLFLGVT
GLILVRAPLP EIQTLVAALS RIPGMSRVLP SRRPLPSDEQ PNEEDQSRRL SAQELAAREA
IALDHMMAGV ALPPLAAGRV RGPRLVPGAP LLEGRYRLLA DHGGWSAARF WQGRELATGD
IVALTIMDPV AYARSQVSPG VSVPVNGVEV ARAKDEMLRL SAKLKQFDVP GMAQVNRVID
YGNLVVIVSR WVQGSPLTTV AESKPEPLAA AFAVSSLADA AAQAEDSGTS LGLDHRDRVR
IGTDGAAVLA FPGVLPNDDT AQDAHGVAVA LRLLLEHVPY EEVPEDLTRI YKKIHELDGE
KVGPEDLRKV AKDLRELKAG GLAIEEDQTP DPSAKSGFGA RGNRPVGMAA AAAIAFVSVL
VVAALVAAVI SVVGGDRKDS PLSTDSLRQG AQAVRGVDPA EVPLSRPLEW LPADVNWPLD
RPDLARLITD GDPETFWQSN PASTQLGGQP GTTKPGIGLL MTLPEGTALS QVQLRGLTQG
TTLELRLAQA DNNGKLGSLD QTTLLKSVQA DSTDVTVDLA GMGADSPGTT GGSSWDNNRE
GSSSTSTESA DGSGDGGSEK GSEKGKYDTD KVSAAKGNRL LIWITGLPLP KPATLAEITA
VGNWLDQTSD ENSGAGEGGI GGANDGANTE ESSRPTRSVQ PVG
//
