ID U5LH12_9BACI Unreviewed; 431 AA.
AC U5LH12;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=N288_20095 {ECO:0000313|EMBL:AGX05892.1};
OS Bacillus infantis NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX05892.1, ECO:0000313|Proteomes:UP000017805};
RN [1] {ECO:0000313|EMBL:AGX05892.1, ECO:0000313|Proteomes:UP000017805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX05892.1,
RC ECO:0000313|Proteomes:UP000017805};
RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT potential to induce cardiac disease by antigenic mimicry.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; CP006643; AGX05892.1; -; Genomic_DNA.
DR AlphaFoldDB; U5LH12; -.
DR STRING; 1367477.N288_20095; -.
DR KEGG; bif:N288_20095; -.
DR PATRIC; fig|1367477.3.peg.4023; -.
DR HOGENOM; CLU_582340_0_0_9; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000017805; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01435; Peptidase_M48; 2.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000017805};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 15..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..155
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT DOMAIN 163..245
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 307..339
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 340..372
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 373..405
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 431 AA; 47873 MW; 8F13DF770F8109AB CRC64;
MNHSLREQLV HRKESLYFAF VILFGILTYL LLSITIIGII MLAILLTATI ILHGLMMAGI
RRNGVKLGEK QFPELYGKAV SVAGQMGLAK VPDIYIVESE GVLNAFASRF FRKNMVVLYS
GIFELIEQKA EKEVLFVLAH EFAHLKRRHV TVSFLLLPAL WVPFLGNAYL RACEYTCDRY
AAYYTESYEA SRNALTMLAI GKELYKKVDQ ETYMEQIESE QGIFIWLNEK LSTHPHLPKR
LHALAQFFAP ETALVLKEKR STVWIGSIAA VLFLALAGTG LWFGLKGIEN LDMLSDMPID
GPVEEVEGIT PLMEAAETSD LASIENQIGN GADINAADSE GSTALHWAVY SGQADAARLL
AEHGADPNTV DAYDTTPLMS AVFADDASMA ELLLEYGADP LYTDAEGLTA YDYAQEYGNP
EVLEVLKPYY E
//
