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Database: UniProt
Entry: B1VI22_CORU7
LinkDB: B1VI22_CORU7
Original site: B1VI22_CORU7 
ID   B1VI22_CORU7            Unreviewed;       397 AA.
AC   B1VI22;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Putative membrane-associated serine protease {ECO:0000313|EMBL:CAQ05822.1};
GN   OrderedLocusNames=cu1863 {ECO:0000313|EMBL:CAQ05822.1};
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ05822.1, ECO:0000313|Proteomes:UP000001727};
RN   [1] {ECO:0000313|EMBL:CAQ05822.1, ECO:0000313|Proteomes:UP000001727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AM942444; CAQ05822.1; -; Genomic_DNA.
DR   RefSeq; WP_012361097.1; NC_010545.1.
DR   AlphaFoldDB; B1VI22; -.
DR   STRING; 504474.cu1863; -.
DR   MEROPS; S01.513; -.
DR   GeneID; 60604644; -.
DR   KEGG; cur:cu1863; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_043139_0_0_11; -.
DR   Proteomes; UP000001727; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR003825; Colicin-V_CvpA.
DR   InterPro; IPR047680; MarP-like.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; NF033740; MarP_fam_protase; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   PANTHER; PTHR43019:SF36; SERINE PROTEASE RV3671C; 1.
DR   Pfam; PF02674; Colicin_V; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CAQ05822.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:CAQ05822.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001727};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   397 AA;  41916 MW;  B69F8F4601769578 CRC64;
     MIVDIALVIC ALAAFFSGLR QGGVAALLSL AGVLIGGYLG LQAVGPVVRL IQDEGTEGSR
     LVIALLTLAA CVVIGYLLGS GIGQRIRDNI RTRQLYRADS AVGSLVAVVT AMVVMWMIAV
     PVLSSQDSRI AREAQDSRII ATIGEVAPNW MRTLPARINA LINRSEIPAV TDPFASVTKR
     EVQPPDPALQ DLPDVAAIGP SVVKVEGIAE QCSRMQQGTG FVVEPGVVMT NAHVVAGTNK
     VTLSTVNGPV DTDVVFYDPE HDIALLRATG ELPLQPLRWA DKPAVSGDDA IALGYPLGGP
     FKAAPVRVRE QMRIAGPNIY ANQRVEREAY SLRGKIVQGN SGGPLVAPNG EVLGLIFGAD
     SNEADTGYAL TKKEVLERVG DTARWSSPVD TRSCVAD
//
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