DIPM_CAUVN
ID DIPM_CAUVN Reviewed; 609 AA.
AC A0A0H3C9Q9;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Cell division protein DipM {ECO:0000305};
DE AltName: Full=Division and polarity-related metallopeptidase {ECO:0000303|PubMed:20497502};
DE AltName: Full=Division involved peptidase carrying LysM domains {ECO:0000303|PubMed:20497504};
DE AltName: Full=Division involved protein with LysM domains {ECO:0000303|PubMed:20497503};
DE Flags: Precursor;
GN Name=dipM {ECO:0000303|PubMed:20497502, ECO:0000303|PubMed:20497503,
GN ECO:0000303|PubMed:20497504};
GN OrderedLocusNames=CCNA_02075 {ECO:0000312|EMBL:ACL95540.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=20497504; DOI=10.1111/j.1365-2958.2010.07222.x;
RA Goley E.D., Comolli L.R., Fero K.E., Downing K.H., Shapiro L.;
RT "DipM links peptidoglycan remodelling to outer membrane organization in
RT Caulobacter.";
RL Mol. Microbiol. 77:56-73(2010).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=20497503; DOI=10.1111/j.1365-2958.2010.07223.x;
RA Poggio S., Takacs C.N., Vollmer W., Jacobs-Wagner C.;
RT "A protein critical for cell constriction in the Gram-negative bacterium
RT Caulobacter crescentus localizes at the division site through its
RT peptidoglycan-binding LysM domains.";
RL Mol. Microbiol. 77:74-89(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=20497502; DOI=10.1111/j.1365-2958.2010.07224.x;
RA Moell A., Schlimpert S., Briegel A., Jensen G.J., Thanbichler M.;
RT "DipM, a new factor required for peptidoglycan remodelling during cell
RT division in Caulobacter crescentus.";
RL Mol. Microbiol. 77:90-107(2010).
RN [5]
RP FUNCTION.
RX PubMed=28833791; DOI=10.1111/mmi.13775;
RA Zielinska A., Billini M., Moell A., Kremer K., Briegel A.,
RA Izquierdo Martinez A., Jensen G.J., Thanbichler M.;
RT "LytM factors affect the recruitment of autolysins to the cell division
RT site in Caulobacter crescentus.";
RL Mol. Microbiol. 106:419-438(2017).
CC -!- FUNCTION: Required for efficient cell division, cell polarity and
CC normal cell morphology (PubMed:20497504, PubMed:20497503,
CC PubMed:20497502). Facilitates remodeling of the peptidoglycan layer
CC and, thus, coordinated constriction of the cell envelope during the
CC division process (PubMed:20497502, PubMed:20497504). Plays a critical
CC role in maintaining proper cell envelope architecture during growth and
CC division (PubMed:20497504). Required for normal envelope invagination
CC during cell division and to establish or maintain outer membrane
CC connections throughout the cell envelope (PubMed:20497504). May serve
CC as a regulatory hub coordinating the activities of multiple
CC peptidoglycan-degrading enzymes during cell constriction. Required to
CC position SdpA and SdpB at midcell (PubMed:28833791).
CC {ECO:0000269|PubMed:20497502, ECO:0000269|PubMed:20497503,
CC ECO:0000269|PubMed:20497504, ECO:0000269|PubMed:28833791}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:20497502,
CC ECO:0000269|PubMed:20497503, ECO:0000269|PubMed:20497504}.
CC Note=Localizes to the division site in an FtsZ-dependent manner during
CC early stages of the division process (PubMed:20497504, PubMed:20497503,
CC PubMed:20497502). Localization also depends on FtsN (PubMed:20497502).
CC {ECO:0000269|PubMed:20497502, ECO:0000269|PubMed:20497503,
CC ECO:0000269|PubMed:20497504}.
CC -!- DOMAIN: Composed of four peptidoglycan binding (LysM) domains and a C-
CC terminal lysostaphin-like (LytM) peptidase domain. The LysM domains are
CC the major mediators of the localization to the division site, probably
CC via direct interaction with peptidoglycans. The LytM region is
CC dispensable for localization, but is essential for function.
CC {ECO:0000269|PubMed:20497502, ECO:0000269|PubMed:20497503,
CC ECO:0000269|PubMed:20497504}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant exhibits morphological defects,
CC including cell widening and filamentation, and cell division defects
CC (PubMed:20497504, PubMed:20497503, PubMed:20497502). Inactivation
CC causes severe defects in outer membrane invagination, resulting in a
CC significant delay between cytoplasmic compartmentalization and final
CC separation of the daughter cells (PubMed:20497502). Cells lacking the
CC gene also show outer membrane blebbing at the division site, at cell
CC poles and along the cell body (PubMed:20497504).
CC {ECO:0000269|PubMed:20497502, ECO:0000269|PubMed:20497503,
CC ECO:0000269|PubMed:20497504}.
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DR EMBL; CP001340; ACL95540.1; -; Genomic_DNA.
DR RefSeq; WP_010919862.1; NC_011916.1.
DR RefSeq; YP_002517448.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C9Q9; -.
DR SMR; A0A0H3C9Q9; -.
DR EnsemblBacteria; ACL95540; ACL95540; CCNA_02075.
DR GeneID; 7330381; -.
DR KEGG; ccs:CCNA_02075; -.
DR PATRIC; fig|565050.3.peg.2033; -.
DR HOGENOM; CLU_029425_0_0_5; -.
DR OMA; ANGYKGP; -.
DR OrthoDB; 1891666at2; -.
DR PhylomeDB; A0A0H3C9Q9; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 4.
DR Gene3D; 2.70.70.10; -; 1.
DR Gene3D; 3.10.350.10; -; 4.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01476; LysM; 4.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 4.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF54106; SSF54106; 4.
DR PROSITE; PS51782; LYSM; 4.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Periplasm; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..609
FT /note="Cell division protein DipM"
FT /evidence="ECO:0000255"
FT /id="PRO_5002606068"
FT DOMAIN 121..165
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 171..215
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 295..339
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 345..389
FT /note="LysM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 21..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..603
FT /note="LytM"
FT /evidence="ECO:0000305|PubMed:20497504"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 63072 MW; 6C6EFA0C426BB3B4 CRC64;
MRQLWTQAAV IALTAGTLGA PAHASGQSGQ RFTPNFPITQ PAAPPPGETI QAQPGEAESL
PRPTPIPVQS APPIAQAELP PPAPVSTPAP APQPVLRATP PRTVVTTTVT GPVVEVAGKP
QVRVVESGDA LDAIARGMGS TRAELVKLND LEPPYRLKLG QKIKGPATTA KAYVVQTGDT
MFAIAKRFNV TAAALAEEND LKSGAAIKKG QKLLLPDGYK DKGPIKTTQV IPGTPATMVA
EAEPAPATTR PATPAATPSR PVRQPVSEET SEPATTSTTT LSVTGSVVTV AGPRQVHTVK
SGDTLTAIAR KFDMSVSELA EANKLDTEKP LKLGAKIKGP ATTQKAYSVQ TGDTLGEIAK
RFNVSVKALA AENNLRATAS LKKGQKIALP DGFRDKGPIR TTTTTRPATP PANTYARVDS
SAAAASTPSS PVPYTPSGAA PRPSAPVAAQ PITPPPSSGR TIIETAAAPT EAEIIASGKG
KFAWPLRGDI ISSFGVKGTG QRNDGLNIRA PQGTPVLSSA DGEIAYAGNQ VPTFGNLVLV
KHADGWVTAY AHLSSTNVKM RQQVKQGEQL GTVGATGGVN EPQLHFEMRY APTVKDKAKP
VDPALVLPR
