MVINL_MYCTO
ID MVINL_MYCTO Reviewed; 1184 AA.
AC P9WJK2; L0TE53; O05435; Q7D4M1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Probable peptidoglycan biosynthesis protein MviN {ECO:0000250|UniProtKB:P9WJK3};
GN Name=mviN; OrderedLocusNames=MT4029;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Essential for cell growth and peptidoglycan synthesis.
CC {ECO:0000250|UniProtKB:P9WJK3}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WJK3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Phosphorylated by PknB. {ECO:0000250|UniProtKB:P9WJK3}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MurJ/MviN family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK48394.1; -; Genomic_DNA.
DR PIR; G70600; G70600.
DR RefSeq; WP_003902580.1; NZ_KK341228.1.
DR AlphaFoldDB; P9WJK2; -.
DR SMR; P9WJK2; -.
DR EnsemblBacteria; AAK48394; AAK48394; MT4029.
DR KEGG; mtc:MT4029; -.
DR PATRIC; fig|83331.31.peg.4335; -.
DR HOGENOM; CLU_006797_0_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004268; MurJ.
DR Pfam; PF03023; MurJ; 1.
DR PRINTS; PR01806; VIRFACTRMVIN.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR01695; murJ_mviN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell shape; Membrane; Peptidoglycan synthesis;
KW Phosphoprotein; Transmembrane; Transmembrane helix.
FT CHAIN 1..1184
FT /note="Probable peptidoglycan biosynthesis protein MviN"
FT /id="PRO_0000427815"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1001..1184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 557..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 947
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P9WJK3"
SQ SEQUENCE 1184 AA; 123564 MW; ECFCB70ED1443464 CRC64;
MRPSPGEVPT ASQRQPELSD AALVSHSWAM AFATLISRIT GFARIVLLAA ILGAALASSF
SVANQLPNLV AALVLEATFT AIFVPVLARA EQDDPDGGAA FVRRLVTLAT TLLLGATTLS
VLAAPLLVRL MLGTNPQVNE PLTTAFAYLL LPQVLVYGLS SVFMAILNTR NVFGPPAWAP
VVNNVVAIAT LAVYLAVPGE LSVDPVRMGN AKLLVLGIGT TAGVFAQTAV LLVAIRREHI
SLRPLWGIDQ RLKRFGAMAA AMVLYVLISQ LGLVVGNRIA STAAASGPAI YNYTWLVLML
PFGMIGVTVL TVVMPRLSRN AAADDTPAVL ADLSLATRLT MITLIPTVAF MTVGGPAIGS
ALFAYGNFGD VDAGYLGAAI ALSAFTLIPY ALVLLQLRVF YAREQPWTPI TIIVVITGVK
ILGSLLAPHI TGDPQLVAAY LGLANGLGFL AGTIVGYYIL RRALRPDGGQ LIGVGEARTV
LVTVAASLLA GLLAHVADRL LGLSELTAHA GSVGSLLRLS VLALIMLPIL AAVTLCARVP
EARAALDAVR ARIRSRRLKT GPQTQNVLDQ SSRPGPVTYP ERRRLAPPRG KSVVHEPIRR
RPPEQVARAG RAKGPEVIDR PSENASFGAA SGAELPRPVA DELQLDAPAG RDPGPVSRPH
PSDLQNGDLP ADAARGPIAF DALREPDRES SAPPDDVQLV PGARIANGRY RLLIFHGGVP
PLQFWQALDT ALDRQVALTF VDPQGVLPDD VLQETLSRTL RLSRIDKPGV ARVLDVVHTR
AGGLVVAEWI RGGSLQEVAD TSPSPVGAIR AMQSLAAAAD AAHRAGVALS IDHPSRVRVS
IDGDVVLAYP ATMPDANPQD DIRGIGASLY ALLVNRWPLP EAGVRSGLAP AERDTAGQPI
EPADIDRDIP FQISAVAARS VQGDGGIRSA STLLNLMQQA TAVADRTEVL GPIDEAPVSA
APRTSAPNSE TYTRRRRNLL IGIGAGAAVL MVALLVLASV LSRIFGDVSG GLNKDELGLN
APTASTSAAS SAPPGSVVKP TKVTVFSPDG GADNPGEADL AIDGNPATSW KTDIYTDPVP
FPSFKNGVGL MLQLPQATVV GTVAIDVAST GTKVEIRSAS TPTPATLEDT AVLTSATALR
PGHNTISVEA AAPTSNLLVW ISTLGTTDGK SQADISEITI YAAS
