ID A1UPB6_MYCSK Unreviewed; 1184 AA. AC A1UPB6; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 95. DE SubName: Full=Integral membrane protein MviN {ECO:0000313|EMBL:ABL94674.1}; DE Flags: Precursor; GN OrderedLocusNames=Mkms_5489 {ECO:0000313|EMBL:ABL94674.1}; OS Mycobacterium sp. (strain KMS). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL94674.1}; RN [1] {ECO:0000313|EMBL:ABL94674.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMS {ECO:0000313|EMBL:ABL94674.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., RA Richardson P.; RT "Complete sequence of chromosome of Mycobacterium sp. KMS."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000518; ABL94674.1; -; Genomic_DNA. DR AlphaFoldDB; A1UPB6; -. DR STRING; 189918.Mkms_5489; -. DR KEGG; mkm:Mkms_5489; -. DR HOGENOM; CLU_006797_0_1_11; -. 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; 2.60.120.260; Galactose-binding domain-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 12..34 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 40..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 71..96 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 116..137 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 149..168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..206 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 226..246 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 266..285 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 306..334 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 378..402 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 408..431 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 443..467 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 487..508 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 978..1000 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 529..677 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 943..972 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1116..1144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 601..615 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 620..634 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 956..972 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1184 AA; 123090 MW; 0F682851D6FBE1E3 CRC64; MAVATLVSRI TGFLRIVLLA AILGAALSSS FTVANQLPNL VAALVLEATF TAIFVPVLAR AERDDPDGGT AFVRRLVTLA TTLLLAATVL SVAGAPLLVR LMLGDDPQVN NPLTTAFAYL LLPQVLFYGL SSVFMAILNT RNVFGPPAWA PVVNNVVAIA TLVLYLIVPG ELSVDPVEMG NAKLLVLGIG TTLGVFAQTA VLLVAIRRER ISLRPLWGID DRLKKFGTMA AAMVLYVLIS QIGLIVTNQI ASASAASGPA IYNYTWLVLM LPFGMIGVTV LTVVMPRLSR NAAADDIPAV LGDLSLATRL TMVTLIPIVA VMTVGGPAIG TALFAYGNFG ETDAGYLGMA ITLSAFTLIP YALVLLQLRV FYAREQPWTP IIVIIVVTTV KVIASLAAPA MTDDPELVAG YLGLANGLGF LAGAVVGHFL LKSSLRPPGG RMFDVQVIRT ILVTIAASLL AGLLAHVADQ LLGLESLTAD AGGVGSLVRL AVLGLIMVPV IAGVLLAARV PEADAAVAFV RRRLGRSAPA PAASISRPDQ PRPAGAFPYS DGRSARPVRR SRGPATGRYD PPVRGTPVHG AGAERWRGPA VSDDSAGDSA AAPDSASTTR ISRPAADTHT RPAAETHSRP AADDFQPDVP ETPSAPADRS ATAEMPTSGR PPADYGGDPT RESLPFDAPR EPAIEAATSD EDVHLIPGAT ISGGRYRLLV FHGGPPNLQF WQALDTALDR QVALTFVDPD ATLPDERVQD ILARTLKLSR LDMPGVARVL DVANTGSGGL IVSEWIRGGS LAEVAETAPS PIGGARAIQS LAAAAEAAHR AGVALSIDHP SRVRVSIEGD VALAFPATMP DATPEDDIRG IGAALYALLV NRWPLPETGV PSGLAPADRD PAGDPLEPRA VDREIPFQIS AAAAHAVQPD GGIRSAPTLL NLLQQATAVA DRTDLISPVD RPDGGTPSRF RGEPDDDPEA QARRKRGLMV GLTVGGVIVV VALIVLATVL SRIFGDVGGG FDGDELGLNA PTTSEEAEGG STAPGNVVRP VRATVFSPAG GADSPDQAGN AIDGNSTTVW PTDIYSDPNP FPNFKNGVGL MLELPQPTTI SSVDVNVSST GTSVQIRSAQ SAEPSSLEST TEMTPSTPLS TGNNTIEVSD ASPTSFVLVW IDKLGTVNGE SRTDISEITL KGTS //