ID I4EUG7_9ACTN Unreviewed; 377 AA.
AC I4EUG7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Protease with a role in cell division {ECO:0000313|EMBL:CCH87030.1};
GN Name=envC {ECO:0000313|EMBL:CCH87030.1};
GN OrderedLocusNames=MODMU_1586 {ECO:0000313|EMBL:CCH87030.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87030.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87030.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87030.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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DR EMBL; FO203431; CCH87030.1; -; Genomic_DNA.
DR RefSeq; WP_014739632.1; NC_017955.1.
DR AlphaFoldDB; I4EUG7; -.
DR STRING; 477641.MODMU_1586; -.
DR KEGG; mmar:MODMU_1586; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_029425_3_5_11; -.
DR OMA; VISEYYD; -.
DR OrthoDB; 1099523at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF270; MUREIN DD-ENDOPEPTIDASE MEPM; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000313|EMBL:CCH87030.1};
KW Cell division {ECO:0000313|EMBL:CCH87030.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CCH87030.1};
KW Protease {ECO:0000313|EMBL:CCH87030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..377
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003689133"
FT DOMAIN 267..359
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT COILED 33..109
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 192..226
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 377 AA; 38588 MW; 35313AC8290F586B CRC64;
MIPTVAIAGL LVGGGAPSAL AAPNVAGQDQ PGRDALTAEI ERINQRLATT EEELQRATVE
AEATADASRA AQAELAAAES AAAAATAELE AAQAAASQAQ DDVATLGREA FMGSAPLGET
VVLLDAAGPE EVLQRAATMD LLGEDRAARL EASEAVRQRQ EDADRAARDA VAERDAAVRA
AADADAAAQA QLAASQQAYD AAAAEKAGLE QQLKDAETRL LAARGATDPN ATWEQQQRTR
LAQASAGAGA LVNGRVTSCY GSRWGTNHNG IDIAAPIGTP IFAPESGVVL QAGPANGFGL
AVYLQHPDGT ITVYGHINQY FVTAGQTVTA GQQIAEVGNK GQVTGPHLHI ETHTGGLYQN
RVDPAPWLAA RGISLGC
//