ID A0A220RZ07_9NEIS Unreviewed; 328 AA.
AC A0A220RZ07;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:ASK26439.1};
GN ORFNames=BG910_00570 {ECO:0000313|EMBL:ASK26439.1};
OS Neisseria chenwenguii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1853278 {ECO:0000313|EMBL:ASK26439.1, ECO:0000313|Proteomes:UP000198238};
RN [1] {ECO:0000313|EMBL:ASK26439.1, ECO:0000313|Proteomes:UP000198238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10023 {ECO:0000313|EMBL:ASK26439.1,
RC ECO:0000313|Proteomes:UP000198238};
RA Zhang G.;
RT "Neisseria chenwenguii sp. nov., isolated from the intestinal contents of
RT Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP022278; ASK26439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220RZ07; -.
DR KEGG; nei:BG910_00570; -.
DR Proteomes; UP000198238; Chromosome.
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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000198238};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 5..22
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 42..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 94..315
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 328 AA; 36695 MW; 37875E434BEC8634 CRC64;
MSLNILYAAI AAFVAGLVLY AVSSKERNEN GEWGSGLQWG YLMMMVGVFG VLSYFMSFTA
VLLVFVAFTG VVWLVHKGRL KKDPNHIDRG HFTDYMSGFF PIILVVFVLR TFVAEPFQIP
SSSMRPGLVV GDFILVNKFA YGIRTPVINN VLIETGKIEH GDVVVFNYPE NPSINYIKRA
VGLPGDVVEY KNKILSINGQ AVGDQAEGAQ SYAENTRQYG TVEIKTEAFR EQIGSHSFQV
LKMADQPSFI PQAVRPAFPY RENCEYAADG SSFKCTVPEG QYFMMGDNRD NSEDSRYWGF
VSDKLVVGKA FFVWMNFGDF SRIGKSIQ
//
