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Database: UniProt
Entry: A0A0C5V4G5_9GAMM
LinkDB: A0A0C5V4G5_9GAMM
Original site: A0A0C5V4G5_9GAMM 
ID   A0A0C5V4G5_9GAMM        Unreviewed;       648 AA.
AC   A0A0C5V4G5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:AJQ94370.1};
GN   ORFNames=YC6258_02332 {ECO:0000313|EMBL:AJQ94370.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ94370.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ94370.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ94370.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CP007142; AJQ94370.1; -; Genomic_DNA.
DR   RefSeq; WP_044616906.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5V4G5; -.
DR   STRING; 1445510.YC6258_02332; -.
DR   KEGG; gsn:YC6258_02332; -.
DR   PATRIC; fig|1445510.3.peg.2288; -.
DR   HOGENOM; CLU_024494_0_0_6; -.
DR   OrthoDB; 15218at2; -.
DR   Proteomes; UP000032266; 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; cd07340; M48B_Htpx_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AJQ94370.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        17..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          114..337
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   648 AA;  72771 MW;  A193A07E968886E6 CRC64;
     MDFFEHQDRA RRNTWKLILF FVTATLLIVM AVNALAFTVW LSWQNHTSYP HLSIPLGFQQ
     WLNNPNAWFT AGATILILLS GSLLQWLNLA KGGEAVARMA DARPIEEFFN DPKATQFRNV
     VAEMAIASGV SAPKLYIMDR ETGINAFVAG YQVNQAVMVV TRGMLTHLNR EQIQGVVGHE
     FSHILNGDMR LNIRLMSMLA GIVMIGQFGR FMADIGGRSG YRSRRSRNNN SALPVFLAGL
     ALMAIGAIGV FFGRLIRAAV SRQREFLADA SSVQFTRNPE AVAGALYKIQ KQSEGSLLQH
     RHAEDMSHFC FGNTVHIAHF NHLLATHPPL PERIKRIAPN FLARQRNIEN RDLENTPQQN
     QAPEATLIGG MAAAVTGLQI QQVVGQTSAA HVDYAHQLYK QIPPYVRTLL ATSAGARAFC
     YGVILKENDQ QQEIVRFIAS EDPNGAENLA RLWKWQRQAA PALRLPCLEL CIPALNKHTV
     EDILIFLQRI QRLCEWDQQI VLMEWIVLSL LDHHLNPAHK TRDKVKHHSL KNLGEELQLL
     LSSLVYLNTD LQKANNAYKQ AMTSMGFADR WLLSRTAIPL TRLQPVMTEL NGLSFILKKT
     VIQACSDIIL SDQQVNVSEY DCLRTIATVF GCPMPPLILE KEQLFGVH
//
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