ID C6ACJ5_BARGA Unreviewed; 270 AA.
AC C6ACJ5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=lebB {ECO:0000313|EMBL:ACS50907.1};
GN OrderedLocusNames=Bgr_05910 {ECO:0000313|EMBL:ACS50907.1};
OS Bartonella grahamii (strain as4aup).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS50907.1, ECO:0000313|Proteomes:UP000001489};
RN [1] {ECO:0000313|EMBL:ACS50907.1, ECO:0000313|Proteomes:UP000001489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT "Run-off replication of host-adaptability genes is associated with gene
RT transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL PLoS Genet. 5:E1000546-E1000546(2009).
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}.
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DR EMBL; CP001562; ACS50907.1; -; Genomic_DNA.
DR RefSeq; WP_012754935.1; NC_012846.1.
DR AlphaFoldDB; C6ACJ5; -.
DR STRING; 634504.Bgr_05910; -.
DR MEROPS; S26.001; -.
DR KEGG; bgr:Bgr_05910; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_2_5; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000001489; 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 Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 17..222
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 270 AA; 30903 MW; 815179D54C1CA0A6 CRC64;
MIQKDKVHKK EKKGGVREFI SVLVQALLLA AVIRTLFFQP FSIPSGSMRP TLLVGDYLFV
SKYAYGYSRF SIPFSPPLFS GRIWASQPQR GDVVVFRLPS NPKIDYIKRV VGLPGDRIQV
RQSVLYINDE AVSRHFMGEI DNSDITEVNY PVEVYRETMP NGVSYDTLDL AFIPKVDDTT
VFEVPQGHYF MMGDNRDNSD DSRLDVGYVP EENLIGRASV IFFSISNGSS AWQVWRWPFD
VRWKRLFSFI NTVHDLPLIK QGNNDETSND
//
