ID D4BRK3_BIFBR Unreviewed; 477 AA.
AC D4BRK3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Serine proteinase inhibitor {ECO:0000313|EMBL:EFE88848.1};
GN ORFNames=BIFBRE_04739 {ECO:0000313|EMBL:EFE88848.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE88848.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE88848.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE88848.1,
RC ECO:0000313|Proteomes:UP000003191};
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., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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:EFE88848.1}.
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DR EMBL; ACCG02000012; EFE88848.1; -; Genomic_DNA.
DR RefSeq; WP_003830341.1; NZ_JDUD01000008.1.
DR AlphaFoldDB; D4BRK3; -.
DR STRING; 1685.RY69_486; -.
DR MEROPS; I04.075; -.
DR GeneID; 69565192; -.
DR KEGG; bbrd:BBBR_1376; -.
DR PATRIC; fig|518634.20.peg.1444; -.
DR HOGENOM; CLU_023330_0_4_11; -.
DR Proteomes; UP000003191; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461:SF211; ACCESSORY GLAND PROTEIN ACP76A-RELATED; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003191};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..470
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 477 AA; 51480 MW; 9101D322E19BC8A9 CRC64;
MMHEPIQAKG LTMSEKLMEQ YRLRKQRKRR NACIAAIVTV VLVLAVAGGV WWTAGDGSVL
VRNMFKPKAT PATQPVVDST AAFAYRTAPE FLAMETGDRD TGNVNYSPAS MWMALAIAAQ
GANGTTRSQL NELLGSGSLA DSDYQSLLSS INGQYSGAKS EMSAANSLWI DNDYSPASDY
QSTVKKMFEA EVTTLPFDDQ AAAKMSDWIA KHTNGSLKPK ITLRDREVLS IINTVYADGR
WKDPFEEQST GDGTFHGEAG DAQVPMMHRT FSQMTYSHDE YNTWQRVEIP FDNGGNLAIV
LPAEGHFDEL AGDAQKLGWA FGTCSSASPG EDAMGCAADS LPGWGVSVNS ATVNVMLPRF
TIDSMFDSEA TIKAFEKLGV TDAFSAGDAD FTKMVDTDSH GENLYIGSIL QGTRIEVNEA
GAKAMSFTKA GADFTSAPVD NIEFTVDRPF LYSYVTPDGI PLFIGAVRNL GGVGGEH
//
