ID Q5E2A0_ALIF1 Unreviewed; 381 AA.
AC Q5E2A0;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Protease with a role in cell division {ECO:0000313|EMBL:AAW86846.1};
GN Name=envC {ECO:0000313|EMBL:AAW86846.1};
GN OrderedLocusNames=VF_2351 {ECO:0000313|EMBL:AAW86846.1};
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86846.1, ECO:0000313|Proteomes:UP000000537};
RN [1] {ECO:0000313|EMBL:AAW86846.1, ECO:0000313|Proteomes:UP000000537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537};
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000020; AAW86846.1; -; Genomic_DNA.
DR RefSeq; WP_011262746.1; NC_006840.2.
DR RefSeq; YP_205734.1; NC_006840.2.
DR AlphaFoldDB; Q5E2A0; -.
DR STRING; 312309.VF_2351; -.
DR EnsemblBacteria; AAW86846; AAW86846; VF_2351.
DR KEGG; vfi:VF_2351; -.
DR PATRIC; fig|312309.11.peg.2390; -.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_4_0_6; -.
DR OrthoDB; 9784703at2; -.
DR Proteomes; UP000000537; Chromosome I.
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; 6.10.250.3150; -; 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:SF265; MUREIN HYDROLASE ACTIVATOR ENVC; 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:AAW86846.1};
KW Cell division {ECO:0000313|EMBL:AAW86846.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AAW86846.1};
KW Protease {ECO:0000313|EMBL:AAW86846.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000537};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..381
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004255397"
FT DOMAIN 282..375
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT COILED 38..107
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 161..191
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 381 AA; 43008 MW; 6DAFCBC1ED69F8CF CRC64;
MNISLLNNSF FCRRLATTAL VCLAFSSPIL VHASDAELKG MKQEISRQNT VLSKQKKELS
SLQNSLKKHE VSIANASKKI RNAEQELTTL KSSISSLKQQ QSELTQQQIG QTEILKDLLV
NYYLTSRNNQ LSNVLSGDDV TKMDRMTQYA QRISEARVGA ISQLEFTNMQ LEEKEADLLE
KQQRQSELLA QYKKEKVTLQ TSQNKRKKTV SSIRKRITNE SSYLNELQQN EKRLKTAIAK
AKAKNNVPMD GIGRQKGRLP WPISNPKTLH SFGTKQTGQL TWKGMVLAGD YGTPVKAVYS
GKVVFADWLR GYGLMVLIDH GKGDMTLYGY NQSLMKKEGD KVRAGETIAV VGDSGGQDRP
SLYFEIRRNS KAQNPRSWLR R
//
