ID Q0BXH2_HYPNA Unreviewed; 363 AA.
AC Q0BXH2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Trypsin domain lipoprotein {ECO:0000313|EMBL:ABI75431.1};
GN OrderedLocusNames=HNE_3146 {ECO:0000313|EMBL:ABI75431.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI75431.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI75431.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI75431.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP000158; ABI75431.1; -; Genomic_DNA.
DR RefSeq; WP_011648117.1; NC_008358.1.
DR AlphaFoldDB; Q0BXH2; -.
DR STRING; 228405.HNE_3146; -.
DR KEGG; hne:HNE_3146; -.
DR eggNOG; COG5640; Bacteria.
DR HOGENOM; CLU_762422_0_0_5; -.
DR Proteomes; UP000001959; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Lipoprotein {ECO:0000313|EMBL:ABI75431.1};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000001959};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004169512"
FT DOMAIN 21..304
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 312..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 37309 MW; C908EC57330BACFD CRC64;
MKSYFKLAVG TAVLATLSGC MVAGRDADIS DWPGMASVQT VSGATIYHEC GATMIAPEWA
LTAAHCVENA RIESNGRAAQ YLEGDTGGMT RFGTLAVAAG LGDLTVIPKG SVFPVREIVL
HPGYQPAMPE KGNDLALLRI AGRWDGPLMP LDGVSGTAGD LMQPYADIVA AGYGKVGETA
QGEEGIARGG RHVRAPSLIL QEGYVPAVDA SVCDSQIRAR INEAGLAAVY PDISIDPATQ
ICAGIGGSDA CQGDSGGPLV LRSSSREPVQ AGIVSWGMGC ARTESPGVYM RVSAFAPWIS
DVTEIALPSQ TPVSDALSGE MPAPEQDEPV TPAPEAVVEP AAEVPPIPAD GPAPEETAQD
TGN
//
