ID B6JGG0_AFIC5 Unreviewed; 253 AA. AC B6JGG0; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 97. 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=lepB1 {ECO:0000313|EMBL:AEI06879.1}; GN OrderedLocusNames=OCA5_c21760 {ECO:0000313|EMBL:AEI06879.1}; OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) OS (Oligotropha carboxidovorans). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Afipia. OX NCBI_TaxID=504832 {ECO:0000313|EMBL:AEI06879.1, ECO:0000313|Proteomes:UP000007730}; RN [1] {ECO:0000313|EMBL:AEI06879.1, ECO:0000313|Proteomes:UP000007730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5 RC {ECO:0000313|Proteomes:UP000007730}; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002826; AEI06879.1; -; Genomic_DNA. DR RefSeq; WP_012562993.1; NC_015684.1. DR AlphaFoldDB; B6JGG0; -. DR STRING; 504832.OCA5_c21760; -. DR MEROPS; S26.001; -. DR KEGG; ocg:OCA5_c21760; -. DR PATRIC; fig|504832.7.peg.2298; -. DR eggNOG; COG0681; Bacteria. DR HOGENOM; CLU_028723_1_2_5; -. DR OrthoDB; 9815782at2; -. DR Proteomes; UP000007730; 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; 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. DR PROSITE; PS00761; SPASE_I_3; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:AEI06879.1}; KW Membrane {ECO:0000256|RuleBase:RU003993}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993}; KW Reference proteome {ECO:0000313|Proteomes:UP000007730}; KW Transmembrane {ECO:0000256|RuleBase:RU003993}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}. FT TRANSMEM 16..35 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003993" FT DOMAIN 15..225 FT /note="Peptidase S26" FT /evidence="ECO:0000259|Pfam:PF10502" FT ACT_SITE 44 FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1" FT ACT_SITE 105 FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1" SQ SEQUENCE 253 AA; 28338 MW; C525CFDC7BE06F18 CRC64; MSATSGTKSE GGIGEAIRVV IHALIIAAVI RTFLFQPFNI PSGSMESTLL VGDYLFVSKY SYGYSHYSLP FSPPLFSGRI FGSAPERGDI VVFRFPREDN IDYIKRVIGL PGDRIQLKEG QVFINDAAVK RERVADYVGE DPCGSGDATA RVKQWQETLP NGVSYKTLDC VDNGFYDNTA VYVVPDGHYF MMGDNRDNSS DSRVMSGVGY VPEQNLIGRA QLIFFSVDRG EQAWQFWRWP VSVRWGRLFS VVR //