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Database: UniProt
Entry: I4EUG7_9ACTN
LinkDB: I4EUG7_9ACTN
Original site: I4EUG7_9ACTN 
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
//
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