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Database: UniProt
Entry: F2BCI7_9NEIS
LinkDB: F2BCI7_9NEIS
Original site: F2BCI7_9NEIS 
ID   F2BCI7_9NEIS            Unreviewed;       352 AA.
AC   F2BCI7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   Name=lepB2 {ECO:0000313|EMBL:EGF10971.1};
GN   ORFNames=HMPREF9123_1442 {ECO:0000313|EMBL:EGF10971.1};
OS   Neisseria bacilliformis ATCC BAA-1200.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=888742 {ECO:0000313|EMBL:EGF10971.1, ECO:0000313|Proteomes:UP000004105};
RN   [1] {ECO:0000313|EMBL:EGF10971.1, ECO:0000313|Proteomes:UP000004105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1200 {ECO:0000313|EMBL:EGF10971.1,
RC   ECO:0000313|Proteomes:UP000004105};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU362042};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362042}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGF10971.1}.
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DR   EMBL; AFAY01000029; EGF10971.1; -; Genomic_DNA.
DR   RefSeq; WP_007342451.1; NZ_GL878494.1.
DR   AlphaFoldDB; F2BCI7; -.
DR   STRING; 267212.GCA_001063965_00292; -.
DR   MEROPS; S26.001; -.
DR   HOGENOM; CLU_028723_1_1_4; -.
DR   OrthoDB; 9815782at2; -.
DR   Proteomes; UP000004105; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EGF10971.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004105};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        47..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          108..338
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   352 AA;  38882 MW;  3C0EDCC23B23004F CRC64;
     MNQFVYLAVA ALVAGIGLFA VSSKERNEKG EWSDSLQWGY LLTMVGVFGL LAVKLSFTAV
     LLIFTVFTGA VWLWRKFSFK PTRNVAIDDK GQKVLTGSLD DDNHFRDYMG GFFPIILVVF
     VLRTFVAEPF QIPSSSMRPG LVKGDFILVN KFAYGIRTPV INNVLLDTGK VERGDVVVFN
     YPLEDANYIK RAVGLPGDTV EYKDKILKVN GNVVETDTEA GGYAYPHDEE PQTQVDTQRF
     HAAFAGRSFD VLKAQDDPAV QTGSLGYYAK LAAEKGMSAQ TDALRQNCTY EADGSGFTCK
     VPAGSYFMMG DNRDHSADSR YWGFVEDKLI VGKAFFIWLN LGEPGRIGSG IL
//
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