ID D3QA66_STANL Unreviewed; 397 AA.
AC D3QA66;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Colicin V production protein {ECO:0000313|EMBL:ADD40778.1};
GN OrderedLocusNames=Snas_1068 {ECO:0000313|EMBL:ADD40778.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD40778.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD40778.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001778; ADD40778.1; -; Genomic_DNA.
DR AlphaFoldDB; D3QA66; -.
DR STRING; 446470.Snas_1068; -.
DR MEROPS; S01.513; -.
DR KEGG; sna:Snas_1068; -.
DR eggNOG; COG0265; Bacteria.
DR eggNOG; COG1286; Bacteria.
DR HOGENOM; CLU_043139_0_0_11; -.
DR Proteomes; UP000000844; 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:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000844};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 397 AA; 41404 MW; BF530B87C5321915 CRC64;
MQGGILVDIV IVLLALLFAI NGYRQGFIIG ALGFAGFFGG ALIGVQIAPL LVEVSEAPAA
RVLIALLVVF GIAMLGQWGG SALGVRLRKR VKNDNAKRFD EFGGALVSMV AVLLVAWVVA
APLASSGMPG LAAAVRNSAI VRTIDENMPG PAQNVYNALR SAVNTNGFPE VFSGLDPSDS
PPVDPPDPEL ANSKVVRDAE ASVLRVSGDA PQCDRHIEGS SFVYDADRDL VLTNAHVVAG
TESVSVAGAD GDVEARVVVF DDRRDLAVLY APGLNAPELD TLDEAAESGA DTIVLGYPQG
GPYTATASRV REHREVTGPD IYDSGEVTRE VYSLRSQVRS GNSGGPLISA DGDVYGVIFA
AAVDDPDTGY AVTMDEARPI MEEGQTTTES VSTKGCT
//
