ID A0A2A9CW16_9ACTN Unreviewed; 1156 AA.
AC A0A2A9CW16;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Murein biosynthesis integral membrane protein MurJ {ECO:0000313|EMBL:PFG18215.1};
GN ORFNames=ATK74_2799 {ECO:0000313|EMBL:PFG18215.1};
OS Propionicimonas paludicola.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Propionicimonas.
OX NCBI_TaxID=185243 {ECO:0000313|EMBL:PFG18215.1, ECO:0000313|Proteomes:UP000226079};
RN [1] {ECO:0000313|EMBL:PFG18215.1, ECO:0000313|Proteomes:UP000226079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15597 {ECO:0000313|EMBL:PFG18215.1,
RC ECO:0000313|Proteomes:UP000226079};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG18215.1}.
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DR EMBL; PDJC01000001; PFG18215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9CW16; -.
DR OrthoDB; 9786339at2; -.
DR Proteomes; UP000226079; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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 InterPro; IPR000719; Prot_kinase_dom.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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:UP000226079};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 626..872
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 558..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 122637 MW; 2D3ACBCAB75EF44F CRC64;
MSEATNSGRK LLSATAVMAS GTMVSRVLGL IRAVLIAFIL GNFTMRADVL TLALTVPSSL
YLLLAGGTLN NVLVPQIVRA VTRDEDGGRA FVDRIMTGFL LILGALTVVF TVAAPLVMSV
YTKSSWRAPE MAEHWRALLL MSYLTMPQIF FYGVFFLIGQ VLNAREKFGP MMWAPVLNNV
VSIISLSAYL FFWGAQTSRD LPFTDQQVWL LGIGSTVGIA VQTLILLPYL RRAGFNYRPR
FDLKGTGLGR TFHVAKWMVG YVALTSLAQV VVTNMASAGG VNAYQQAYLI WILPHSLLTV
SLATAMLPAA STAALAGDLA GVAAETNRAL RLALTFLVPA SVAFVALADP IARVPFGNGA
GASDYHYVAW ALAAFGIGLV PYTIQYLYLR AFYALDNTKT PFGLQIWISG ANATLAVAFV
LAWNDPNTVA ARLALAYSVS YFLGVFLTYR SLKRRLPELD GRSLWQQLAR LLLASAPAAL
VGWLITWAGA GLASSWLRLL VLAVAGAAAV AVFVLVARRL GIDEVSSLLS MLRRKHGDDG
EADAAEVLVA EEDAELSGEV PLEEHGRPAD YERPEPPRAD INPDTDPDGI GVFVQVTPLP
PPPEAILEYP EPSVDPGTGR VLAGRYRLGT LLAASAAGQS WLGQDIVLGR PVLVQLLPSG
APRTAAVLRS ARQAAGATDA RFLRVLDVVV PDLTDQASLL DQTDEPPEGA FVVYEYAAGQ
TLAKLLRRGP LTGVETAWVI REIADAINGL HAQGQHHGQL NPATVLITNS GNLKILGYAA
GLDDAAPGTE AGDILALGEL LYACLVARWP MEAAFGLHPV LEKDGRLPLP SEVRNGVAPQ
LDKIVDRLLS VEPRGHAAPI ETASELTTQL SLVLGPTSAV SDLRARLNRN ADELDSPAPV
SRVAPPLPTP AASRFQMTVP VDGSSAESGD EEEFVASALD RQEGFTPVPP PPVSAPEAPE
PRKPRLPFVI GTFGLVLAVG LLAAATLTGN PVVVPTTAPP VKLTIIAADD FDPKDDGGSG
AENPKLVLQA IDGNPKTSWV SEKYKKTGNF GGTKPGVGLI VDLGTIREVT TVEVMSTDPG
GAVQVMVPNE SPTAAPKRSV TQWHAVATAA DLAADTLLAP SAPVRSRYLL VYLTSLPSIG
KSVYQGTISE IAVLGR
//
