ID X5EGC2_9CORY Unreviewed; 1145 AA.
AC X5EGC2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:AHW65646.1};
GN ORFNames=CGLY_16050 {ECO:0000313|EMBL:AHW65646.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW65646.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW65646.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW65646.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP006842; AHW65646.1; -; Genomic_DNA.
DR RefSeq; WP_052540493.1; NZ_CP006842.1.
DR AlphaFoldDB; X5EGC2; -.
DR STRING; 1404245.CGLY_16050; -.
DR KEGG; cgy:CGLY_16050; -.
DR eggNOG; COG0728; Bacteria.
DR HOGENOM; CLU_006797_0_1_11; -.
DR Proteomes; UP000023703; 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:UP000023703};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 119395 MW; 56ADEC2FBFCC0C4C CRC64;
MTDSREDPGD AAHTGERGRF RAATPPAKAA PSRSSRSSGS TDHDTSDATG GTDSGADHSK
LNMSPAERAA TDPRLTKATA AASKTTSSSG ASITEAADGN EGSGATTASD TDVVRATGSM
AIATLLSRIT GFLRTALIGW ALGAGVASAF NTANTLPNLI TELVLGAVLT SLVVPLLVRA
EKEDSDRGAA FIRRLLTLTF TLMMTVTVIA VLAAPLLTRV SLDSDGQVNI GMSTAFAYLV
LPQIVFYALF AVMMAVLNTK GIFKPGAWAP VVNNVVTLAV LSLYILLPNE SKLGKDDVVT
ITDPHIMLLG LGTTLGVVVQ AAIMVPYLRK AGVDIRPLWG LDDRLKQFGG MALAIVVYVL
ISQIGWVLNN RIASSSGAGP TIYMQAWQLL QVPYGVIGVT LLTAVMPRLS RNAADGDDKA
VVKDLTMATK LTMLALVPVI AFFTAFGTLI APALFAYQEF SLDDANVLGW TISFSAFTLV
PYAIVLLHLR VFYAREEVWT PTFIIGGITI TKVSLAYLAP HIASEPRLVV VLLGAANGMG
FVAGAIIGHR LLKRSLGHLG MRSVLKTSLW ALGASAVSAL IVWRLDALVD RFLIPDGFMF
GFLLRLMIAG VVFLAIVMLI MSRSKLPEVM TVGATLARLP VVGRFFAGAV PEDEDGRPAA
RITEMPIAGM AGLTGQDVVG PAMPPLSAGR VRGPRLVPGA PILQGRFRLL SDHGGSPAAR
LWQARDNETG DLVALTILDP QVAGVGSREL LDRSATLAKV SSPGVARVRE ICDARTLVVV
VADWTDGAPL TRVAESGPDP LAAGYAMADL ADAAGDVADL GGSLGIDHRN RLRISSEGRA
VLAFPGVLPG GSSRQDVHAI AVSLDMLLSS VPSHLIPAEL QQILDDARQV DGVDARQLAT
RLRAATTSES PDADLVTSAD VAPNPEQRAG FGAAPEKPGR TALSVTLTIA GLFLIVALIV
VVVAYFGGDR RDSPVTTDSI RGGQSTSAQA AAEPEPVGVS DASEWAPAES GTGTLDNPED
APLVIDGDPA TTWSSAQYVD QLGDGPSSLK PGIGLLLSLD EAASVTSVDL EGVPDGTRIE
LRSGSGDITA VDQTELVDAE TASGGTLTLS GEDAPTGDRV LLWITELPMP EAASVGEVTV
HGVRE
//
