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Database: UniProt
Entry: C4GGC9_9NEIS
LinkDB: C4GGC9_9NEIS
Original site: C4GGC9_9NEIS 
ID   C4GGC9_9NEIS            Unreviewed;       338 AA.
AC   C4GGC9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=lepB {ECO:0000313|EMBL:EEP69284.1};
GN   ORFNames=GCWU000324_01197 {ECO:0000313|EMBL:EEP69284.1};
OS   Kingella oralis ATCC 51147.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Kingella.
OX   NCBI_TaxID=629741 {ECO:0000313|EMBL:EEP69284.1, ECO:0000313|Proteomes:UP000003009};
RN   [1] {ECO:0000313|EMBL:EEP69284.1, ECO:0000313|Proteomes:UP000003009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51147 {ECO:0000313|EMBL:EEP69284.1,
RC   ECO:0000313|Proteomes:UP000003009};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) 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:EEP69284.1}.
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DR   EMBL; ACJW02000002; EEP69284.1; -; Genomic_DNA.
DR   RefSeq; WP_003795289.1; NZ_GG665871.1.
DR   AlphaFoldDB; C4GGC9; -.
DR   STRING; 629741.GCWU000324_01197; -.
DR   MEROPS; S26.001; -.
DR   GeneID; 84906563; -.
DR   HOGENOM; CLU_028723_1_1_4; -.
DR   OrthoDB; 9815782at2; -.
DR   Proteomes; UP000003009; 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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EEP69284.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003009};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        43..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          95..324
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   338 AA;  37482 MW;  05D4751716453F69 CRC64;
     MNTNFILYGA IALFIVGIIM LATSNKNRLA TGDWSNTLQW GYLLMMIGVF GILSAGLAWS
     FTAVLLLFTA FTGAIWLWQK LSHKDKIKPD NNHLRDYMAG FFPIIAVVFV VRTFIVEPFQ
     IPSSSMRSGL VKGDFILVNK FSYGIRVPVL NTVAVPTGSI QRGDVVVFNY PVEPQNNYIK
     RIVAVGGDTV EYKDKILTVN GKASVDVPQG GYTYPDDGNS NIPRQAERFQ STFEGKTFDV
     LKVDGAPSVD APTWNHYQAM FAQTGFESGL QQNCEYAEDG SGFKCKVPAG KYFAMGDNRD
     NSADSRYWGF VDDKLIVGKA FMIWLNTGEM SRVGTIIK
//
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