ID A0A3A9ZDW4_9ACTN Unreviewed; 585 AA.
AC A0A3A9ZDW4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Murein biosynthesis integral membrane protein MurJ {ECO:0000313|EMBL:RKN46325.1};
GN Name=murJ {ECO:0000313|EMBL:RKN46325.1};
GN ORFNames=D7223_15525 {ECO:0000313|EMBL:RKN46325.1};
OS Micromonospora endolithica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN46325.1, ECO:0000313|Proteomes:UP000281726};
RN [1] {ECO:0000313|EMBL:RKN46325.1, ECO:0000313|Proteomes:UP000281726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN46325.1,
RC ECO:0000313|Proteomes:UP000281726};
RX PubMed=15046305; DOI=10.1078/072320204322881781;
RA Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT Micromonospora endolithica sp. nov. and two isolates related to
RT Micromonospora coerulea Jensen 1932.";
RL Syst. Appl. Microbiol. 27:166-174(2004).
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:RKN46325.1}.
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DR EMBL; RBAK01000005; RKN46325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9ZDW4; -.
DR OrthoDB; 9786339at2; -.
DR Proteomes; UP000281726; 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 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.
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:UP000281726};
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..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 60592 MW; 6B1EA3484658B9A9 CRC64;
MSGGLYRSAN AAQGGGTPGD QRPSDGATFI SAEPLNQPAL ESTAPPQEQV AEASAATNSA
MMAVLSLVSR GTGFLRNLVI GAALGGALVG DAYTTAQILP GMVYEFLLGG ILTSVLIPVL
VRRRKTDADG GQAYAQRLLT LAVLALGVAA LLAVALASPL TWLYGGDESA PGYSGLVTAL
ARLMLPMIFF SGLSALISAV LNTRGHFAAP MWAPILNNLV VIGTAGLYIA IFGAEIVRPE
DMTTGRVLLI GGGTLLGVSI QAAGLLPALR KVGFRWKLRF DFRKLGLAEL GRLGAWMICY
VAVSQVGLIV LINLLNRAGN ENAAGPLIYN NVFLLLMTAH GIIAVSIITA LMPRMSAAAA
DGRFADLTAD LSRGTRTVSA VLAPIAVCYA VLATPIAFTL FRIGAFTEEN ATATSLVLLA
AAVALVPFAI SQLFTFAFYA LPDTRTPALI NIPVVALRIG VQIVLYVALS ATFVGAGMMI
GNAVSYLAAA IASAWLLRPR VGRIGLGDIL RTLGRVALAA LGAALAGLLV VKLLPGDDTP
TRLEAIVQLV VGGAVIGGTY LGLAMVLRIR EITDVIGMVR GRLGR
//
