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Database: UniProt
Entry: A0A1H0GJA1_9BACI
LinkDB: A0A1H0GJA1_9BACI
Original site: A0A1H0GJA1_9BACI 
ID   A0A1H0GJA1_9BACI        Unreviewed;      1457 AA.
AC   A0A1H0GJA1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:SDO06910.1};
GN   ORFNames=SAMN04488053_106130 {ECO:0000313|EMBL:SDO06910.1};
OS   Alkalicoccus daliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=745820 {ECO:0000313|EMBL:SDO06910.1, ECO:0000313|Proteomes:UP000198778};
RN   [1] {ECO:0000313|Proteomes:UP000198778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10369 {ECO:0000313|Proteomes:UP000198778};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010860}.
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DR   EMBL; FNIL01000006; SDO06910.1; -; Genomic_DNA.
DR   STRING; 745820.SAMN04488053_106130; -.
DR   OrthoDB; 363232at2; -.
DR   Proteomes; UP000198778; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 8.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF01471; PG_binding_1; 8.
DR   Pfam; PF08239; SH3_3; 3.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 3.
DR   SUPFAM; SSF47090; PGBD-like; 8.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51781; SH3B; 3.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198778};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011724780"
FT   DOMAIN          1058..1120
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          1128..1190
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          1199..1270
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   REGION          240..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..309
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..330
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..408
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1457 AA;  158125 MW;  6CF486BE7785EC87 CRC64;
     MKKHRLKQAG ITGLASLLFL SSALPATAGS MEDLYEDLFP ELSDEESSLE VSPSLFNQSF
     EEALHISYEE GIEDVSLGLF EEESGTLLGE LEVTPIDATK AAWEFQVTQE DVTEEVILED
     QRYFIEVLTD EEAEEEIETA QVSFVHYSEL PVLSWEESEE LEELELGGQA YSALQEFGLD
     PGELSLSFEA EGLEEAEEVS IEEDGSFNVD VSFLSETTSL YFTLADPLGN TLEEEKLVTI
     EEDTDTSFEE ENADADESTL ENEEDASPAE EEITEAKESE ETALEEETEK KEESSNEEET
     DVSEENTSTE EVVNEEKNED VSEEEELTSE ETTEKEKSTE KSSNEEETDV SEENTSTEDV
     VNEEKNEDVS EEEELTSKET TEKEKSTEKS STEEETDVSE ENTSTEDIVN EENTDAAKST
     AENEEAVNET TASEETEETF STFSTFSMQA TEAPAEEYYD GASGEYIREL KFDLTALGFG
     NFPSYPSTRF GPVTMGVVED FQRAYGLPVT GIPDQATLDA IENALNEETK ETISSFSTQA
     TKASEGEFYD GASGEYIREL KLDLTALGFG NFPSYPSTRF GPVTMGVVED FQKANGLNIT
     GIPDSITLKT IDSALNSNFY SGATGDYVTD LKINLTKLGF GNFPESPSSL FGPVTMSVVE
     DFQKAHGLAV TGIPDAATLD AMNVALSTTF YNGASGEYVR NLKLDLTKLG FGSFPESPSS
     LFGPVTMSVV EDFQKAHGLA VTGIPDAATL DAMNVALSTT FYNGASGEYV RNLKLDLTKL
     GFGSFPESPS SLFGPVTMRV VEDFQKAKGL AATGIPDTAT LQAMDLALKT AFYNGASGEH
     VRTLKLDLTK LGYGSFPSSP SAAFGNVTMK VVEDFQKANN LKVTGIPDSA TLKSINDQLE
     ILANTTYEPG SSGVHVQELK KKLTLLGFGS FPSNPSIYYG SVTKKVVEEF QKYYGVKVTG
     IGDKSTFNKI EELFKSPLSP GNSNTQTVEL KNNLTKLGYG SFPTNPSRVY GSVTSSVVKD
     FQKKNSLAIN GIADGPTLQK INSQLNNQPK EEIKPVVIET GEVTATALNI RSGPGTSHDR
     VGTLTNGTVV EILGEESGWY LIKFDGGTAY ASGSFIDTTK KEAAPKVIDT GKVTATTLNI
     RSGPGTSHDR VGTLTNGTVV EILGEENGWY LIKFDGGTAY ASGSFIDTSK LPAPGNDFTG
     SSIIAYTNGS SLNVRSGPST AYRVLDNLGS NTRVEIISTR ASSGSDTWHQ IRYDGGKTGF
     VSAGYLQLAT KASARTGPLA GKKIVLDAGH GGHDSGGIGG GMLEKDVVLD ITNRAEELLR
     AAGAEVIMLR RTDFFLALGQ RSFMANRSGA DVFLSIHTNM FNGQARGTET FWHDRYERSN
     SIRLANAVQD ATVAKMGTHY RRVDYGNYSV IRQTEIPSAL LEIGFKDHPD DAAKLRSNTY
     RQRAAEAIRD GMINYFK
//
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