MVINL_MYCTU
ID MVINL_MYCTU Reviewed; 1184 AA.
AC P9WJK3; 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 43.
DE RecName: Full=Probable peptidoglycan biosynthesis protein MviN {ECO:0000305};
GN Name=mviN; OrderedLocusNames=Rv3910;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 678-963, FUNCTION, ACTIVITY
RP REGULATION, SUBUNIT, INTERACTION WITH FHAA, DOMAIN, PHOSPHORYLATION AT
RP THR-947, AND MUTAGENESIS OF THR-947.
RX PubMed=22275220; DOI=10.1126/scisignal.2002525;
RA Gee C.L., Papavinasasundaram K.G., Blair S.R., Baer C.E., Falick A.M.,
RA King D.S., Griffin J.E., Venghatakrishnan H., Zukauskas A., Wei J.R.,
RA Dhiman R.K., Crick D.C., Rubin E.J., Sassetti C.M., Alber T.;
RT "A phosphorylated pseudokinase complex controls cell wall synthesis in
RT mycobacteria.";
RL Sci. Signal. 5:RA7-RA7(2012).
CC -!- FUNCTION: Essential for cell growth and peptidoglycan synthesis.
CC {ECO:0000269|PubMed:22275220}.
CC -!- ACTIVITY REGULATION: Probably regulated via interaction with FhaA.
CC {ECO:0000269|PubMed:22275220}.
CC -!- SUBUNIT: Homodimer. Interacts with the FHA domain of FhaA.
CC {ECO:0000269|PubMed:22275220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The extendend C-terminal region contains a kinase-like region,
CC which encodes a catalytically inactive pseudokinase, and an
CC extracellular region reminiscent of carbohydrate-binding proteins.
CC {ECO:0000269|PubMed:22275220}.
CC -!- PTM: Phosphorylated by PknB. Phosphorylation recruits FhaA.
CC {ECO:0000269|PubMed:22275220}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MurJ/MviN family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46739.1; -; Genomic_DNA.
DR PIR; G70600; G70600.
DR RefSeq; NP_218427.1; NC_000962.3.
DR RefSeq; WP_003902580.1; NZ_NVQJ01000005.1.
DR PDB; 3OTV; X-ray; 3.09 A; A/B/C/D=679-963.
DR PDB; 3OUK; X-ray; 3.40 A; A=679-963.
DR PDB; 3OUN; X-ray; 2.70 A; B=676-963.
DR PDB; 3UQC; X-ray; 2.26 A; A/B/C/D=678-963.
DR PDBsum; 3OTV; -.
DR PDBsum; 3OUK; -.
DR PDBsum; 3OUN; -.
DR PDBsum; 3UQC; -.
DR AlphaFoldDB; P9WJK3; -.
DR SMR; P9WJK3; -.
DR STRING; 83332.Rv3910; -.
DR iPTMnet; P9WJK3; -.
DR PaxDb; P9WJK3; -.
DR PRIDE; P9WJK3; -.
DR DNASU; 886247; -.
DR GeneID; 886247; -.
DR KEGG; mtu:Rv3910; -.
DR TubercuList; Rv3910; -.
DR eggNOG; COG0728; Bacteria.
DR OMA; VSRSWGM; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR GO; GO:0034204; P:lipid translocation; IBA:GO_Central.
DR GO; GO:0015836; P:lipid-linked peptidoglycan transport; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell shape; Membrane;
KW Peptidoglycan synthesis; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1184
FT /note="Probable peptidoglycan biosynthesis protein MviN"
FT /id="PRO_0000419663"
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 947
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22275220"
FT MUTAGEN 947
FT /note="T->A: Abolishes phosphorylation by PknB."
FT /evidence="ECO:0000269|PubMed:22275220"
FT TURN 706..709
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 710..719
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 723..729
FT /evidence="ECO:0007829|PDB:3UQC"
FT TURN 730..733
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 749..763
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:3OUK"
FT STRAND 773..779
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 782..788
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 795..799
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 805..824
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:3UQC"
FT TURN 841..843
FT /evidence="ECO:0007829|PDB:3OUK"
FT STRAND 845..847
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 858..874
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:3UQC"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:3OUN"
FT HELIX 902..905
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 911..921
FT /evidence="ECO:0007829|PDB:3UQC"
FT HELIX 930..941
FT /evidence="ECO:0007829|PDB:3UQC"
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
