ID A0A248JQZ7_9PROT Unreviewed; 251 AA.
AC A0A248JQZ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN Name=lepB {ECO:0000313|EMBL:ASG20940.1};
GN ORFNames=Y958_09000 {ECO:0000313|EMBL:ASG20940.1};
OS Nitrospirillum amazonense CBAmc.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG20940.1, ECO:0000313|Proteomes:UP000197153};
RN [1] {ECO:0000313|EMBL:ASG20940.1, ECO:0000313|Proteomes:UP000197153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBAmC {ECO:0000313|EMBL:ASG20940.1,
RC ECO:0000313|Proteomes:UP000197153};
RA Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA Magalhaes Cruz L., Baldani J.I.;
RT "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT from sugarcane.";
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:RU003993};
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}.
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DR EMBL; CP022110; ASG20940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248JQZ7; -.
DR KEGG; nao:Y958_09000; -.
DR Proteomes; UP000197153; Chromosome 1.
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; IPR019756; Pept_S26A_signal_pept_1_Ser-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; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000197153};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 6..221
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 251 AA; 27701 MW; 58E650D3EC05C22D CRC64;
MRRAVLEWGR FILIWGVCVL SFRAFAFGSY YVPSESMLPT LAVGDHFIAA KYAYGYSRHS
PDITLPEGFI PTADGRLLSH LPQRGDIVVL KPEGAPEALV KRVIGLPGDT VQLAHGRLVL
NGQVIGRHET GAYDYRDDHG RTVHVTEYVE DLPATDGSLA RHAVLQRSDE GPADNTGVYT
VPAGHVFLMG DNRDNSQDSR FPYPDLGFVP LDRVIARAQF TAYTNHFCKA ESDLTCPGGD
WSTRFGRSLK P
//
