ID A0A1X1SZ93_9MYCO Unreviewed; 1227 AA.
AC A0A1X1SZ93;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Murein biosynthesis protein MurJ {ECO:0000313|EMBL:ORV37033.1};
GN ORFNames=AWC01_16935 {ECO:0000313|EMBL:ORV37033.1};
OS Mycolicibacterium doricum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=126673 {ECO:0000313|EMBL:ORV37033.1, ECO:0000313|Proteomes:UP000193564};
RN [1] {ECO:0000313|EMBL:ORV37033.1, ECO:0000313|Proteomes:UP000193564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44339 {ECO:0000313|EMBL:ORV37033.1,
RC ECO:0000313|Proteomes:UP000193564};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ORV37033.1}.
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DR EMBL; LQOS01000054; ORV37033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1SZ93; -.
DR STRING; 126673.AWC01_16935; -.
DR Proteomes; UP000193564; Unassembled WGS sequence.
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; IPR011009; Kinase-like_dom_sf.
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 PRINTS; PR01806; VIRFACTRMVIN.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:UP000193564};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1043
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 127620 MW; CBB1C640801A3C5C CRC64;
MPPPPGAARP NPARRRPPPP PRQRIPRGPA PRRRAGRPEL SDAAVVSRSW GMAVATLVSR
ITGFLRVVLL AAILGAALAS SFTVANQLPN LVAALVLEAT FTAIFVPVLA RAERDDPDGG
TAFVRRLVTL ASTLLLVATV LSVAGAPLLV HLMLGDDPRV NNPLTTAFAY LLLPQVLFYG
LASVFSAILN TRNVFGPPAW APVVNNVVAI ATLGLYLIVP GELSIDPVEM GNAKLLVLGI
GTTLGVFAQT AVLLVAIRRE RISLRPLWGI DDRLKKFGTM AAAMVLYVLI SQVGLIVGNQ
IASGAAASGP AIYNYTWLVL QLPFGVIGVT VLTVVMPRLS RNAAADNIRA VLGDFSLATR
LTMVTLIPIV AVMTVGGPAI GTALFAYGNF GETDAGYLGM AITLSAFTLI PYALVLLQLR
VFYARERPWT PTIVIVVVTM VKVIASVAAP ALADDPELVA GYLGLANGLG FLAGAVVGHF
LLKSSLRPPG GRMLDVEVIR TILVTTAASL LAGLLAHVAD QLLGLESLTA AGGGAGSLVR
LAVMGLIMIP VIAGVLLAAR VPEAEAAVAF LRRRLGRPAP VPAASISRPH QPLFPDAFPY
SDGRSARPVR RSRGPATGRY ESPVRGTPVR GTEADRWRGP AVSDDSAGDS VAAPDSASTT
KISRPAADHP ARPAADHPAR PAADDFHPDV VESATTEMPM SGRPPADYGG DPTRESLPFD
APREPPVEAA TSDEDVHLIP GATIGGGRYR LLVFHGGPPD LQFWQALDTA LDRQVALTFV
DPDGTLPDES VQDILSRTLK LSRLDMPGVA RVLDVANTGS GGLIVSEWIR GGSLAEVAET
APSPIGGARA MQSLAAAAEA AHRSGVALSI DHPSRVRVSI EGDVALAFPA TMPDATPEDD
IRGIGAALYA LLVNRWPLPE TGVPSRLAPA DQDPAGNPVE PRAVDRAIPF QISAAAVRAV
QPDGGIRSAP TLLNLLQQAT AVADRTDLIS PVDRPDGGAA PAPFHGGPDD AEAQARRRRG
LVVGLTVGGA IVVVALVVLA TVLSRVFGDV DGGFDGDELG LNAPSTSAES EGGTTAPGNV
VRPVRATVFS PDGGADSPDL AGNAIDGSST TVWPTDTYSD PIPFPNFKNG VGLMLELPEP
TTITAVDVNV SSTGTSVQIR SSPSAEPSSL DSTTEMTPST PLRRGKNTIT VSGASPTSYV
LVWIDKLGTV DGESRTDVSE ITLRGTT
//
