ID A0A1X2BEF0_9MYCO Unreviewed; 1177 AA.
AC A0A1X2BEF0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Murein biosynthesis protein MurJ {ECO:0000313|EMBL:ORW61978.1};
GN ORFNames=AWC22_04590 {ECO:0000313|EMBL:ORW61978.1};
OS Mycobacterium riyadhense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=486698 {ECO:0000313|EMBL:ORW61978.1, ECO:0000313|Proteomes:UP000193087};
RN [1] {ECO:0000313|EMBL:ORW61978.1, ECO:0000313|Proteomes:UP000193087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45176 {ECO:0000313|EMBL:ORW61978.1,
RC ECO:0000313|Proteomes:UP000193087};
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:ORW61978.1}.
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DR EMBL; LQPQ01000229; ORW61978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2BEF0; -.
DR STRING; 486698.AWC22_04590; -.
DR Proteomes; UP000193087; 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 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 971..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 554..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 122859 MW; EEC7894F4AD6079E CRC64;
MPPRPGWTPQ QPPQRKPELS DAALVSRSWG MAFATLISRL TGFARIVLLA AILGAALASS
FSVANQLPNL VAALVLEATF TAIFVPVLAR AEQDDPDRGA AFVRRLVTLA TTLLLAATAL
SVLAAPLLVR LMLGRDPQVN EPLTTAFAYL LLPQVLAYGL SAVFMAILNT RNVFGPPAWA
PVVNNVVAIA TLAVYLAVPG ELSVDPVEMG NAKLLVLGIG TTLGVFAQTA VLLIAIGRQH
ISLRPLWGID QRLKRFGAMA AAMVFYVLIS QLGLVVGNQI ASTAAASGPA IYNYTWLVLM
LPFGMIGVTV LTVVMPRLSR NAAANDTPAV LADLSLATRL TMITLIPTVA LMTVGGRAIG
SALFAYGNFG DVDAGYLGAA IALSAFTLIP YALVLLQLRV FYAREQPWTP IVIIVVITTV
KIVGSVLAPH LTSDRELVAG YLGLANGLGF LAGAIGGYVL LRRALRPRGG KLVGVAEVRT
ILVATAASLL ASLIAYLADR LLGLDQLSAH GGGIGSLLRL VVVAMIMLPI VAAVMLRAQV
PEARAALAAV RRRIGGRRGP SKPTAPDGSS RRSQVTYPEQ RNSSLPGPNA VQEPIRRRPP
ATPAGIAKGP EVTDRPSDSA SSHSGPGTER PVADDFQPDI PADLDRGPGS VPRQPERNGD
HVPAPRGPIP FDAPRERGPE PSAPHDEVHL VPGARIANGR YRLLISHGGT PPLQFWQALD
TALDRQVALT FVDPRGTLPD DALQEILSRT LRLSRIDKPG IARVLDVVHT GSGGLVVAEW
IRGGSLQEVA DTSPSPVGAI RAMQSLAAAA DAAHRAGVAL SIDHPSRVRV SIDGDVVLAY
PATMPDANPQ DDIRGIGASL YALLVNRWPL PESGTRSGLA PAQRDAAGNP VEPAIVDRDI
PFQISAVAVR SVQEDGGIRS ASTLLNLLQQ ATAVADRTEI LGPIDEVPPP AAPREPSVRG
AGPFGNRRRN LIIGVTAAAA VILVALLVLA SVLNRMFDLG NGINKDQLGL TAPTSSTSGA
PEASAPPGST VKPTKATVFS PDGEADNPGE AGQAIDGDPG SAWHTDIYTD AVPFPGFKNG
VGLMLQLPKP TVVGAVSLNV SSTGTKVEIR SASSPTPSKL SDTTVLTSAT ALKPGRNTIA
VKTSSPTSNL LVWISTLGTT DGKSRADISE LTIQAAS
//
