ID   D2Q5I5_BIFDB            Unreviewed;       441 AA.
AC   D2Q5I5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Neuroserpin {ECO:0000313|EMBL:ADB10200.1};
GN   OrderedLocusNames=BDP_1607 {ECO:0000313|EMBL:ADB10200.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB10200.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB10200.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   EMBL; CP001750; ADB10200.1; -; Genomic_DNA.
DR   RefSeq; WP_003839325.1; NC_013714.1.
DR   AlphaFoldDB; D2Q5I5; -.
DR   MEROPS; I04.075; -.
DR   GeneID; 69536263; -.
DR   KEGG; bde:BDP_1607; -.
DR   eggNOG; COG4826; Bacteria.
DR   HOGENOM; CLU_023330_0_3_11; -.
DR   Proteomes; UP000008693; Chromosome.
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; IPR023795; Serpin_CS.
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.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008693};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..441
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   441 AA;  48527 MW;  5EAB0E3C04867AAF CRC64;
     MKRIDLRGTT IVTPKSAQRN KAGRRVIIAI IAAVLAIAIV VTGGFWYFAW DGRYTVADLF
     RPKAVAASDA AVESSRSFAY ESAVKFLAKQ KNVNYSPASL QMALLVAAQG AKGDTLSQLQ
     QALASEKLSD SDLTSIYRSI IGKRSGKSRL DAANSIWARR DLTLNKDYTD AVRRIFGTQV
     KRVKAFDNDT NKAMSTWISD QTRGMLKPEI DTPKNNGMSI LNTLYADGRW SDPFDKASTK
     KSTFHTLQGS TSTIDFMHKT FETEQHADDV DAYTKGDGWQ RVDLTFDNGG RMKILLPDNN
     TRFKALRGDA AALRKAFSAK SNAQSDTEVN VSLPKFSIDS TFDSDSMIKA MQEMGVTDAF
     NVDKADFSGM SDARMFIGAI VQGTRIEVTE AGAKAAAYTQ IDMELAMMPV ETVDFNVDRP
     FLYEFDSPDG LPLFIGAVTE L
//