ID A0A1A2MSZ6_9MYCO Unreviewed; 1203 AA.
AC A0A1A2MSZ6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Murein biosynthesis integral membrane protein MurJ {ECO:0000313|EMBL:OBH06024.1};
GN ORFNames=A5695_05935 {ECO:0000313|EMBL:OBH06024.1};
OS Mycobacterium sp. E1747.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH06024.1, ECO:0000313|Proteomes:UP000092218};
RN [1] {ECO:0000313|Proteomes:UP000092218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-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:OBH06024.1}.
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DR EMBL; LZJI01000200; OBH06024.1; -; Genomic_DNA.
DR RefSeq; WP_068086469.1; NZ_LZJI01000200.1.
DR AlphaFoldDB; A0A1A2MSZ6; -.
DR STRING; 1834128.A5695_05935; -.
DR Proteomes; UP000092218; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 125353 MW; 3BDE91CF01032ECB CRC64;
MKPGHRQAAP QPHRLPEPPR RPRSPGSPPT GPLPPVPAGI DRRRPELSDA ALVSRSWAMA
LATLVSRLTG FARIVLLAAI LGAALSSAFS VANQLPNLVA ALVLEATFTA IFVPVLARAE
QSDPDGGAAF VRRLVTLTTA LLVLATALSV LAAPLLVRLM LGRVPQVNEP LTTAFAYLLL
PQVLAYGLTS VFMAILNTRN VFGPTAWAPV VNNVVALATL AVYAAVPGEL SVDPVRMGNT
KLLVLGIGTT LGVFAQTAVL LVALRRQRVD LRPLWGIDER LKRFGTMAAA MVLYVLISQL
GLVVGNQIAS TAAASGPAIY NYTWLVLMLP FGMIGVTVLT VVMPRLSRNA AADDTKAVLA
DLSLATRLTL ITLIPIVAVM TVGGPAIGSA LFAYGHFGGV DAGYLGTAIA LSAFTLIPYG
LVLLQLRVFY AREQPWTPIV IILVITAVKI VGSVLAPHLT DDPKLVAGYL GLANGIGFLA
GAIIGYLLLR HTLLPAGGEL IGKGELRTIL VTITASMLAG LVAHVADRLL GLDALTAHGG
AAGSLLRLLI LAVIMLPIMA AVLLRAGVPE AQAALDVVRR RFGGRAAMSR NPVTKDRSSR
RARVTYPEQR NSSTPGVNAV QEPIRRRPPE RATQARIAKG PEVTDRPIES AASGAELPPP
VADDFQPDIP AERAPEPPAA RPSNGDLPPE SRRGPAPFDA PRDRGADPSG DDVHLVPGAR
IAGGRYRLLV FHGGAPPLQF WQALDTALDR QVALTFVDPD GALPDEVLQE ILSRTLRLSR
IDKPGIARVL DVVHTGHGGL VVSEWVRGGS LQEVADTAPS PVGAVRAMQS LAAAADAAHR
AGVALSIDHP SRVRVSIEGD VVLAYPATMP DANPQADIRG IGAALYALLV NRWPLTESSV
RSGLAPAERD STGQPVEPMI IDRGIPFQIS AVAVRAVQED GGIRSASTLL NLLQQATAVA
DRTEVLGPID DSPAPATARE SAAPDEAAFA RRRRNLLIGM GAGLAVIIVA LLVLASVVSK
IFGNVGGGLN KDELGLNGPS SSTSSSATSS AAAGSVVKPT KATVYSPDGD ADNAGTAGQA
IDGDPSTAWA TEVYTDAVPF PSFKQGEGLM LQLPSATVIG QVSIDTPSTG TKVEIRSSAT
ASPASLNDTT VLAPAFTLRP GHNVIPVRAG SPTSNLLVWI STLGTTNGKS QAGFFEITVQ
AAS
//
